1UKM

Crystal structure of EMS16, an Antagonist of collagen receptor integrin alpha2beta1 (GPIa/IIa)

Summary for 1UKM

• Entry DOI: 10.2210/pdb1ukm/pdb
• Descriptor: EMS16 A chain, EMS16 B chain, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: domain swapping, c-type lectin, toxin
• Biological source: Echis multisquamatus; More
• Total number of polymer chains: 2
• Total formula weight: 31635.96

Authors

Horii, K.,Okuda, D.,Morita, T.,Mizuno, H. (deposition date: 2003-08-27, release date: 2003-11-04, Last modification date: 2025-10-29)

Primary citation

Horii, K.,Okuda, D.,Morita, T.,Mizuno, H.
Structural characterization of EMS16, an Antagonist of collagen receptor (GPIa/IIa) from the venom of Echis multisquamatus
Biochemistry, 42:12497-12502, 2003

PubMed Abstract: 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.

PubMed: 14580195
DOI: 10.1021/bi034890h

Experimental method

X-RAY DIFFRACTION (1.9 Å)