X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution.

Lobsanov, Y.D.; Gitt, Michael A.; Leffler, Hakon; Barondes, Samuel H.; Rini, James M.

doi:10.1016/s0021-9258(19)74214-8

Cited by 242 publications

(67 citation statements)

References 48 publications

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“…2). The topological motif consists of a 'jelly-roll', which results from tight association between a five-stranded (F1-F5) and a six-stranded (S1-S6a/S6b) sheet, as described for galectins -1 and -2 [20][21][22]. The molecule has very little loop structure, with the majority of residues adopting conformation.…”

Section: Structure Descriptionmentioning

confidence: 99%

“…The lectin domain in CLC protein. This domain is compared with bovine spleen galectin-1 complexed with N-acetyl-lactosamine [21]; human galectin-2 complexed lactose [22]; coral tree lectin complexed with lactose [76]; 3-D-glucanase complexed with 3,4-epoxy-butyl-3-D-cellobioside [45]; the N-terminal domain of asparagine amidase [44]; Human serum amyloid P component [48] and Wing-i from Vibrio cholerae neuraminidase [50]. Bound metal ions are shown as green spheres.…”

Section: Similarity To Other Lectin-like Structuresmentioning

confidence: 99%

“…These residues, together with Trp68, form part of the carbohydraterecognition site in galectins. More detailed pictures of galectin-1 complexed with biantennary saccharides [20] and N-acetyl-lactosamine [21], and galectin-2 in complex with lactose [22], have recently been obtained by Xray crystallography. These studies reveal highly conserved carbohydrate-binding sites in the galectins, which differ from the cation-dependent site in legume lectins.…”

Section: The Carbohydrate-recognition Sitementioning

confidence: 99%

“…Indeed, in the CLC protein structure the conformation of this site is very similar to that observed in the galectins involving strands S4, S5, S6a and S6b on the concave face of one 3 sheet. In galectins -1 and -2 [20][21][22] this site consists of seven key residues: His44, Asn46, Arg48, Asn61l, Trp68, Glu71 and Arg73, and the structurally equivalent residues in the CLC protein are His53, Gln55, Cys57, Asn65, Trp72, Gln75 and Glu77 (Figs 3,5). Examination of this site in these proteins reveals that there is a high degree of structural conservation on one side of the carbohydrate-binding groove with the crucial amino-acid changes Arg48 to Cys57 and Arg73 to Glu77 occurring on the other side in the CLC protein (Table 4).…”

Section: The Carbohydrate-recognition Sitementioning

confidence: 99%

“…The galectins are defined by their affinity for P-galactosides and twelve highly conserved residues in their sequence that comprise their carbohydrate-recognition domain. Most of the conserved residues are involved in interaction with bound carbohydrate, as shown by X-ray crystallography of galectins -1 and -2 [20][21][22] and site-directed mutagenesis [23][24][25]. The CLC protein sequence contains seven out of the twelve conserved residues and in addition shares many other residues with the mammalian galectins [9,10].…”

Section: Introductionmentioning

confidence: 99%

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Crystal structure of human Charcot–Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins

et al. 1995

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The CLC protein structure possesses a carbohydrate-recognition domain comprising most, but not all, of the carbohydrate-binding residues that are conserved among the galectins. The protein exhibits specific (albeit weak) carbohydrate-binding activity for simple saccharides including N-acetyl-D-glucosamine and lactose. Despite CLC protein having no significant sequence or structural similarities to other lysophospholipase catalytic triad has also been identified within the CLC structure, making it a unique dual-function polypeptide. These structural findings suggest a potential intracellular and/or extracellular role(s) for the galectin-associated activities of CLC protein in eosinophil and basophil function in allergic diseases and inflammation.

show abstract

Section: Structure Descriptionmentioning

confidence: 99%

Section: Similarity To Other Lectin-like Structuresmentioning

confidence: 99%

Section: The Carbohydrate-recognition Sitementioning

confidence: 99%

Section: The Carbohydrate-recognition Sitementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Crystal structure of human Charcot–Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins

et al. 1995

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Variability in quaternary association of proteins with the same tertiary fold: A case study and rationalization involving legume lectins

1999

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Legume lectins constitute a family of proteins in which small alterations arising from sequence variations in essentially the same tertiary structure lead to large changes in quaternary association. All of them are dimers or tetramers made up of dimers. Dimerization involves side-by-side or back-to-back association of the flat six-membered beta-sheets in the protomers. Variations within these modes of dimerization can be satisfactorily described in terms of angles defining the mutual disposition of the two subunits. In all tetrameric lectins, except peanut lectin, oligomerization involves the back-to-back association of side-by-side dimers. An attempt has been made to rationalize the observed modes of oligomerization in terms of hydrophobic surface area buried on association, interaction energy and shape complementarity, by constructing energy minimised models in each of which the subunit of one legume lectin is fitted in the quaternary structure of another. The results indicate that all the three indices favor and, thus, provide a rationale for the observed arrangements. However, the discrimination provided by buried hydrophobic surface area is marginal in a few instances. The same is true, to a lesser extent, about that provided by shape complementarity. The relative values of interaction energy turns out to be a still better discriminator than the other two indices. Variability in the quaternary association of homologous proteins is a widely observed phenomenon and the present study is relevant to the general problem of protein folding.

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Crystal structure of YbaK protein fromHaemophilus influenzae (HI1434) at 1.8 ? resolution: Functional implications

Zhang

Huang

et al. 2000

Proteins

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Structural genomics of proteins of unknown function most straightforwardly assists with assignment of biochemical activity when the new structure resembles that of proteins whose functions are known. When a new fold is revealed, the universe of known folds is enriched, and once the function is determined by other means, novel structure-function relationships are established. The previously unannotated protein HI1434 from H. influenzae provides a hybrid example of these two paradigms. It is a member of a microbial protein family, labeled in SwissProt as YbaK and ebsC. The crystal structure at 1.8 A resolution reported here reveals a fold that is only remotely related to the C-lectin fold, in particular to endostatin, and thus is not sufficiently similar to imply that YbaK proteins are saccharide binding proteins. However, a crevice that may accommodate a small ligand is evident. The putative binding site contains only one invariant residue, Lys46, which carries a functional group that could play a role in catalysis, indicating that YbaK is probably not an enzyme. Detailed sequence analysis, including a number of newly sequenced microbial organisms, highlights sequence homology to an insertion domain in prolyl-tRNA synthetases (proRS) from prokaryote, a domain whose function is unknown. A HI1434-based model of the insertion domain shows that it should also contain the putative binding site. Being part of a tRNA synthetases, the insertion domain is likely to be involved in oligonucleotide binding, with possible roles in recognition/discrimination or editing of prolyl-tRNA. By analogy, YbaK may also play a role in nucleotide or oligonucleotide binding, the nature of which is yet to be determined.

show abstract

X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution.

Cited by 242 publications

References 48 publications

Crystal structure of human Charcot–Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins

Crystal structure of human Charcot–Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins

Variability in quaternary association of proteins with the same tertiary fold: A case study and rationalization involving legume lectins

Crystal structure of YbaK protein fromHaemophilus influenzae (HI1434) at 1.8 ? resolution: Functional implications

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