Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin 1 1Edited by A. Klug

Manoj, Narayanan; Srinivas, V.R.; Surolia, Avadhesha; Vijayan, M.; Suguna, K.

doi:10.1006/jmbi.2000.4111

Cited by 37 publications

(38 citation statements)

References 54 publications

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“…Accordingly, the roughly-estimated denaturation enthalpy values that are listed in Table 1 must be taken with great caution. The thermodynamic studies on Phaseolus vulgaris leucoagglutinin appeared to be quite different from previous studies on peanut agglutinin (Reddy et al, 1999), Con A (Schwarz et al, 1993), pea seed (Schwarz et al, 1993;Manoj et al, 2000), and lentil lectin (Schwarz et al, 1993), although all of them are composed of canonical dimers and are members of the legume lectin family. The melting temperature of legume lectins that has been reported was below 100 o C [e.g., thermodynamic studies on peanut agglutinin, a homotetrameric legume lectin (Reddy et al, 1999)], which shows that the unfolding process is reversible.…”

Section: Resultscontrasting

confidence: 87%

“…Current thermodynamic studies on Con A (Schwarz et al, 1993), pea seed lectin (Manoj et al, 2000), lentil lectin (Schwarz et al, 1993), and tetrameric peanut agglutinin (Reddy et al, 1999) show that the folding process in these proteins are reversible and cooperative. In the present communication, differential scanning calorimetry (DSC) was used to study the thermal denaturation of the kidney bean (Phaseolus vulgaris) leucoagglutinin as a function of pH that ranges from 2 to 3.…”

Section: Introductionmentioning

confidence: 99%

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Thermal Stability of Phaseolus vulgaris Leucoagglutinin: a Differential Scanning Calorimetry Study

Biswas¹,

Kayastha²

2002

BMB Reports

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Phaseolus vulgaris phytohemagglutinin L is a homotetrameric-leucoagglutinating seed lectin. Its threedimensional structure shows similarity with other members of the legume lectin family. The tetrameric form of this lectin is pH dependent. Gel filtration results showed that the protein exists in its dimeric state at pH 2.5 and as a tetramer at pH 7.2. Contrary to earlier reports on legume lectins that possess canonical dimers, thermal denaturation studies show that the refolding of phytohemagglutinin L at neutral pH is irreversible. Differential scanning calorimetry (DSC) was used to study the denaturation of this lectin as a function of pH that ranged from 2.0 to 3.0. The lectin was found to be extremely thermostable with a transition temperature around 82ºC and above 100ºC at pH 2.5 and 7.2, respectively. The ratio of calorimetric to vant Hoff enthalpy could not be calculated because of its irreversiblefolding behavior. However, from the DSC data, it was discovered that the protein remains in its compact-folded state, even at pH 2.3, with the onset of denaturation occurring at 60ºC.

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Section: Resultscontrasting

confidence: 87%

Section: Introductionmentioning

confidence: 99%

Thermal Stability of Phaseolus vulgaris Leucoagglutinin: a Differential Scanning Calorimetry Study

Biswas¹,

Kayastha²

2002

BMB Reports

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“…However, only after several hours of dialysis PNA monomer folds back from the unfolded state to the tetramer as observed by 85% reversibility of the wavelength maxima. Thus PNA forms an Change in accessible surface area (DASA) has been calculated by NACCESS (30,31). The change in total accessible surface area is 108474 Å 2 of which 64.2% is contributed by non-polar groups and 35.7% is contributed by polar groups.…”

Section: Discussionmentioning

confidence: 99%

Thermodynamic analysis of three state denaturation of Peanut Agglutinin

Dev

Nirmala

Sinha

et al. 2006

IUBMB Life (International Union of Biochemistry and Molecular B

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SummaryPeanut Agglutinin (PNA) is a homotetrameric protein with a very unusual open quaternary structure. During denaturation, it first dissociates into a molten globule like state, which subsequently undergoes complete denaturation. Urea denaturation of PNA at neutral pH has been studied by intrinsic fluorescence spectroscopy and has been fitted to a three state model, A 4 , 4I , 4U, to get all the relevant thermodynamic parameters. Urea denaturation leads to continuous red shift of wavelength maxima. The molten globule like state is formed in a short range of urea concentration. Refolding of the denatured PNA has been attempted by intrinsic fluorescence study. Refolding by instantaneous dilution shows the occurrence of the formation of an intermediate at a relatively rapid rate, within few seconds. The transition from PNA tetramer to molten globule like state is found to have a DG value of *33 kcal/mole while it is *8 kcal/mole for the transition from molten globule like state to a completely denatured state. This in turn indicates that the tetramerization in PNA contributes significantly to the stability of the oligomer. IUBMB Life, 58: 549-555, 2006

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“…9,28,29 One of them, responsible for the different blood group specificities of the two homologous lectins from winged beans, involve variation in loop length. 29 The same strategy appears to be responsible for the difference in the sugar specificities of artocarpin and heltuba. As illustrated in Figure 6, the main difference between the combining sites of artocarpin and heltuba is in the length of the third loop.…”

Section: Specificity Generation In Jacalin-related Mannose Lectinsmentioning

confidence: 99%

Structural Basis for the Carbohydrate Specificities of Artocarpin: Variation in the Length of a Loop as a Strategy for Generating Ligand Specificity

Jeyaprakash

Srivastav

Surolia

et al. 2004

Journal of Molecular Biology

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Artocarpin, a tetrameric lectin of molecular mass 65 kDa, is one of the two lectins extracted from the seeds of jackfruit. The structures of the complexes of artocarpin with mannotriose and mannopentose reported here, together with the structures of artocarpin and its complex with Me-amannose reported earlier, show that the lectin possesses a deep-seated binding site formed by three loops. The binding site can be considered as composed of two subsites; the primary site and the secondary site. Interactions at the primary site composed of two of the loops involve mainly hydrogen bonds, while those at the secondary site comprising the third loop are primarily van der Waals in nature. Mannotriose in its complex with the lectin interacts through all the three mannopyranosyl residues; mannopentose interacts with the protein using at least three of the five mannose residues. The complexes provide a structural explanation for the carbohydrate specificities of artocarpin. A detailed comparison with the sugar complexes of heltuba, the only other mannose-specific jacalinlike lectin with known three-dimensional structure in sugar-bound form, establishes the role of the sugar-binding loop constituting the secondary site, in conferring different specificities at the oligosaccharide level. This loop is four residues longer in artocarpin than in heltuba, providing an instance where variation in loop length is used as a strategy for generating carbohydrate specificity.

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Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin 1 1Edited by A. Klug

Cited by 37 publications

References 54 publications

Thermal Stability of Phaseolus vulgaris Leucoagglutinin: a Differential Scanning Calorimetry Study

Thermal Stability of Phaseolus vulgaris Leucoagglutinin: a Differential Scanning Calorimetry Study

Thermodynamic analysis of three state denaturation of Peanut Agglutinin

Structural Basis for the Carbohydrate Specificities of Artocarpin: Variation in the Length of a Loop as a Strategy for Generating Ligand Specificity

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