1ukm: Difference between revisions

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[[Image:1ukm.gif|left|200px]]
{{Seed}}
[[Image:1ukm.png|left|200px]]


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{{STRUCTURE_1ukm|  PDB=1ukm  |  SCENE=  }}  
{{STRUCTURE_1ukm|  PDB=1ukm  |  SCENE=  }}  


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




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_14580195}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_14580195}}


==About this Structure==
==About this Structure==
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[[Category: C-type lectin]]
[[Category: C-type lectin]]
[[Category: Domain swapping]]
[[Category: Domain swapping]]
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