Interaction of Concanavalin a With Model Substrates*

Goldstein, Irwin J.; Reichert, Cheryl M.; Misaki, Akira

doi:10.1111/j.1749-6632.1974.tb53040.x

Cited by 167 publications

(69 citation statements)

References 63 publications

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“…In order to probe the intermolecular forces dominating such interactions, deoxy-and fluorodeoxy-saccharide analogues have been employed in several specificity studies (2)(3)(4)(5). Such analogues are useful since the hydroxyl moiety is replaced by a smaller, and therefore sterically compatible, substituent, but one of different electronic properties.…”

Section: Introductionmentioning

confidence: 99%

The preferred conformation of 2-fluoro-2-deoxy β-D-mannopyranosyl fluoride. An X-ray crystallographic and 2-dimensional proton nuclear magnetic resonance study

Withers¹,

Street²,

Rettig³

1986

Can. J. Chem.

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STEPHEN G. WITHERS, IAN P. STREET, and STEVEN J. RETTIG. Can. J. Chem. 64, 232 (1986). The preferred conformation of 2-fluoro-2-deoxy P-D-mann~pyran~Syl fluoride has been determined in the solid state by X-ray crystallography and in aqueous solution by 2-dimensional J-resolved proton nuclear magnetic resonance. Crystals of 2-fluoro-2-deoxy P-D-mannopyranosyl fluoride are monoclinic, a 4 10.9150(8), b 4 4.9079(4), c 4 6.9902(6) A, P = 105.158(4)", Z = 2, space group P2]. The structure was solved by direct methods and was refined by full-matrix least-squares procedures to R = 0.028 and R,, = 0.031 for 797 reflections with 1 2 3u(I). The sugar ring was present in an essentially undistorted 4CI chair conformation. Weak, but significant interactions, presumably hydrogen bonding of the type OH . .. 232 (1986). On a dCtermin6 la conformation privilCgiCe du fluorure du fluoro-2 dtoxy-2 P-D-mannopyrannosyle tant a 1'Ctat solide en faisant appel diffraction des rayons-X qu'en solution aqueuse en faisant appel a la rmn du 'H bidimensionnelle rCsolue pour J . Les cristaux du fluoru!e du fluoro-2 dCoxy-2 P-D-mannopyrannosyle sont monocliniques avec a= 10,9150(8), b=4,9079(4), c=6,9902(6) A, P = 105,158(4)", Z=2 et groupe d'espace P2'. On a rCsolu la structure par des methodes directes et on l'a affinCe par la mCthode des moindres carrCs (matrice entikre) jusqu'a des valeurs de R=0,028 et R, = 0,03 1 pour 797 rkflexions avec 1 2 3a(I). Le cycle du sucre existe essentiellement dans une conformation chaise 4~1 qui n'est pas dCformCe. Dans la maille du cristal, on observe des interactions faibles, mais significatives, qui sont probablement dues B des liaisons hydrogknes du type OH. . . F et CH . . . F. Les constantes de couplage observtes dans le spectre rmn du 'H en solution ne peuvent &tre expliqukes que par une conformation chaise 4~I .On discute brikvement de ces rksultats par rapport aux rCsultats obtenus rCcemment concernant l'interaction des sucres fluoro-dCoxy avec les sites de liaison enzymatique.[Traduit par le journal] IntroductionThe mode of interaction of carbohydrates and proteins has been attracting considerable interest of late, particularly since the antigenic determinants of red blood cells are oligosaccharides and it is their interaction with receptor proteins that is central to blood type recognition (1). In order to probe the intermolecular forces dominating such interactions, deoxy-and fluorodeoxy-saccharide analogues have been employed in several specificity studies (2-5). Such analogues are useful since the hydroxyl moiety is replaced by a smaller, and therefore sterically compatible, substituent, but one of different electronic properties. Systematic studies of mono-substituted derivatives can therefore provide information on the factors contributing to binding at each position. The enzyme glycogen phosphorylase provides a useful model system for a study of carbohydrate/ protein interactions since the three-dimensional structure of the glycogen phosphorylase/glucose complex has been determined by X-ray ...

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Section: Introductionmentioning

confidence: 99%

The preferred conformation of 2-fluoro-2-deoxy β-D-mannopyranosyl fluoride. An X-ray crystallographic and 2-dimensional proton nuclear magnetic resonance study

Withers¹,

Street²,

Rettig³

1986

Can. J. Chem.

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“…In comparing the structure of fructose with mannose it is apparently clear that the atoms known to be essential for carbohydrate binding to con A (Goldstein et al, 1974) are present in equivalent positions in fructose to mannose. Why equivalent binding of fructose is not observed is not clear from these structures.…”

Section: 6 Conclusionmentioning

confidence: 99%

“…In the case of a l-2 mannobiose however, méthylation leads to a 3 fold increase in affinity. Goldstein's rules (Goldstein et al, 1974) describe the requirements for monosaccharide binding to con A as being free equatorial hydroxyl groups at the 3-and 4-and 6-positions. Both sugar rings in a l-2 mannobiose can potentially be recognised by the monosaccharide binding site.…”

Section: Introduction -mentioning

confidence: 99%

“…However, inspection of difference electron density reveals that the carbohydrate is present in low occupancy. It is impossible to quantify this as the density is too weak to even model a carbohydrate in to the binding site apart from in one subunit of the P2i2i2i structure.In comparing the structure of fructose with mannose it is apparently clear that the atoms known to be essential for carbohydrate binding to con A (Goldstein et al, 1974) are present in equivalent positions in fructose to mannose. Why equivalent binding of fructose is not observed is not clear from these structures.…”

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“…203 Allen, K. N., Lavie, A., Glasfeld, A., Tanada, T. N., Gerrity, D. P., Carlson, S. C., Farber, G. K., Petsko, G. A. and Ringe, D. (1994) Baneijee, R., Das, K., Ravishankar, R., Suguna, K., Surolia, A. and Vijayan, M. (1996) Conformation , Proteins: Struct., Funct., Genet., 12,[203][204][205][206][207][208][209][210][211][212][213][214][215][216][217][218][219][220][221][222] Goldstein, I. J., Reichert, C. M. and Misaki, A. (1974) Stidy of Concanavalin A: The Proton of Asp28, J. Chem.…”

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Protein-Carbohydrate Interactions

Abbott¹,

Bueren²

2017

Methods in Molecular Biology

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All rights reserved INFORMATION TO ALL USERSThe quality of this reproduction is d e p e n d e n t upon the quality of the copy subm itted.In the unlikely e v e n t that the a u thor did not send a c o m p le te m anuscript and there are missing pages, these will be noted. Also, if m aterial had to be rem oved, a n o te will ind ica te the deletion. uestProQuest 10171019Published by ProQuest LLO (2017). C opyright of the Dissertation is held by the Author. In submitting this thesis to the University of St. Andrews I understand that I am giving permission for it to be made available for use in accordance with the regulations of the University Library for the time being in force, subject to any copyright vested in the work not being affected thereby. I also understand that the title and abstract will be published, and that a copy of the work may be made and supplied to any bona fide library or research worker. 15Acknowledgements.Firstly, thanks go to my supervisor Jim Naismith for his constant enthusiasm and encouragement over the past three years, and for helping me to achieve my goals. Thanks also go to Steve Homans, JTrevor Rutherford, Charlie Weller and Tony Chiovotti for useful discussions. A special thanks goes to everyone in the Naismith group, especiallyStephen for making the lab a good place to work.Thanks are not enough for my parents, they are truly amazing.Finally, a special thanks goes to Alex, who achieved the impossible and made the sun shine every day in St. Andrews. 16Chapter 1Protein -Carbohydrate Interactions. 17 SummaryCarbohydrates are ubiquitous in biological systems. A sophisticated array of these molecules are found on cell surfaces and they are recognised with varying degrees of specificities by carbohydrate binding proteins such as lectins, anti-carbohydrate antibodies, bacterial periplasmic binding proteins and some enzymes. The interactions between proteins and carbohydrates are attractive therapeutic targets. However, the ubiquity of carbohydrates presents a huge challenge for rational design of therapeutics.The physical basis of protein -carbohydrate interactions is still too poorly understood to permit such design. Improving our understanding needs an atomic level understanding of the recognition of a carbohydrate by a protein. In recent years. X-ray crystallography together with isothermal titration microcalorimetry has begun to provide a powerful insight into the molecular processes governing protein -carbohydrate interactions. This chapter will summarise the current information available from X-ray structures and thermodynamics studies, identifying common features of protein -carbohydrate interactions.Concanavalin A from the Jack bean {Canavalia enisform is\ is the most well studied lectin. It was the first of the lectins to have its three dimensional structure solved by Xray crystallography, the first to have a carbohydrate bound structure solved and the first lectin to be solved to atomic resolution. The thermodynamics of its binding to both natural and modified carbohydrates ...

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Ultrastructural localization of concanavalin A‐binding sites in the Golgi apparatus of various types of neurons in rat dorsal root ganglia: Functional implications

Malchiodi¹,

Rambourg²,

Clermont

et al. 1986

Am. J. Anat.

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The localization of concanavalin A (con A) binding sites has been determined at the electron-microscopic level in the six types of neurons (A1, A2, A3, B1, B2, C) of rat dorsal root ganglia. In all ganglion cells, con A stained the plasma membrane, the nuclear envelope, the cisternae of the rough endoplasmic reticulum, and the matrix of some multivesicular bodies. In contrast, the con A reactivity of the Golgi apparatus varied according to cell type. In type B1 and B2 cells and possibly in type A3 cells, the lectin was exclusively located in three or four saccules on the cis side of the Golgi stacks, whereas the TPPase-positive saccules and the trans sacculotubular elements were unstained with con A. In type A1, A2, and C neurons, all Golgi saccules as well as the trans sacculotubular elements were stained with the lectin. These results suggest that different types of glycoproteins were produced in these two groups of neurons. In the type A1, A2, and C cells, the persistence of the lectin reactivity in the TTPase-positive saccules or sacculotubular elements on the trans side of the Golgi stacks suggests the presence of glycoproteins with oligosaccharide side chains rich in alpha-D-mannosyl residues in terminal positions. In contrast, the disappearance of the con A reactivity in equivalent elements of the Golgi stacks in type B1, B2, and A3 cells suggests the addition at this level of other sugar residues characteristic of complex oligosaccharide side chains. The majority of the vesicular elements associated with the Golgi apparatus, as well as lysosomes, were unstained with con A.

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Interaction of Concanavalin a With Model Substrates*

Cited by 167 publications

References 63 publications

The preferred conformation of 2-fluoro-2-deoxy β-D-mannopyranosyl fluoride. An X-ray crystallographic and 2-dimensional proton nuclear magnetic resonance study

The preferred conformation of 2-fluoro-2-deoxy β-D-mannopyranosyl fluoride. An X-ray crystallographic and 2-dimensional proton nuclear magnetic resonance study

Protein-Carbohydrate Interactions

Ultrastructural localization of concanavalin A‐binding sites in the Golgi apparatus of various types of neurons in rat dorsal root ganglia: Functional implications

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