1ukm
From Proteopedia
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Crystal structure of EMS16, an Antagonist of collagen receptor integrin alpha2beta1 (GPIa/IIa)
Overview
Snake venoms contain a number of hemostatically active C-type lectin-like, proteins (CLPs), which affect the blood coagulation system, endothelial, cells, and platelets. CLPs have broad similarities in structure and, possess distinct biological functions. EMS16, a CLP from Echis, multisquamatus venom, which is a potent and selective inhibitor of the, collagen receptor, glycoprotein Ia/IIa (integrin alpha2beta1), has been, used in the present study to examine structure-function relationships in, venom CLPs by X-ray crystallography. The structure of EMS16, determined at, a resolution of 1.9 A, revealed a heterodimer involved with domain, swapping of the central loop as observed in the structures of other CLPs., A part of the glycan was observed and identified as N-acetyl-D-glucosamine, (GlcNAc) in the electron density map at Asn21 of subunit B, an expected, glycosylation site. EMS16 had a unique, positively charged electrostatic, potential patch on the concave surface that may qualify as a site for, interaction with the I-domain of the glycoprotein Ia/IIa.
About this Structure
1UKM is a Protein complex structure of sequences from Echis multisquamatus with NAG, CL and GOL as ligands. Full crystallographic information is available from OCA.
Reference
Structural characterization of EMS16, an antagonist of collagen receptor (GPIa/IIa) from the venom of Echis multisquamatus., Horii K, Okuda D, Morita T, Mizuno H, Biochemistry. 2003 Nov 4;42(43):12497-502. PMID:14580195
Page seeded by OCA on Sun Nov 25 04:08:38 2007
Categories: Echis multisquamatus | Protein complex | Horii, K. | Mizuno, H. | Morita, T. | Okuda, D. | CL | GOL | NAG | C-type lectin | Domain swapping