1f9k
From Proteopedia
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WINGED BEAN ACIDIC LECTIN COMPLEXED WITH METHYL-ALPHA-D-GALACTOSE
Overview
Structures of two crystal forms of the dimeric acidic winged bean, agglutinin (WBAII) complexed with methyl-alpha-D-galactose have been, determined at 3.0 A and 3.3 A resolution. The subunit structure and, dimerisation of the lectin are similar to those of the basic lectin from, winged bean (WBAI) and the lectin from Erythrina corallodendron (EcorL)., The conformation of a loop and its orientation with respect to the rest of, the molecule in WBAII are, however, different from those in all the other, legume lectins of known structure. This difference appears to have been, caused by the formation of two strategically placed salt bridges in the, former. Modelling based on the crystal structures provides a rationale for, the specificity of the lectin, which is very different from that of WBAI, for the H-antigenic determinant responsible for O blood group reactivity., It also leads to a qualitative explanation for the thermodynamic data on, sugar-binding to the lectin, with special emphasis on the role of a, tyrosyl residue in the variable loop in the sugar-binding region in, generating the carbohydrate specificity of WBAII.
About this Structure
1F9K is a Single protein structure of sequence from Psophocarpus tetragonolobus with AMG, MN and CA as ligands. Full crystallographic information is available from OCA.
Reference
Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin., Manoj N, Srinivas VR, Surolia A, Vijayan M, Suguna K, J Mol Biol. 2000 Oct 6;302(5):1129-37. PMID:11183779
Page seeded by OCA on Sat Nov 24 23:31:36 2007
