1ukm
From Proteopedia
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|PDB= 1ukm |SIZE=350|CAPTION= <scene name='initialview01'>1ukm</scene>, resolution 1.90Å | |PDB= 1ukm |SIZE=350|CAPTION= <scene name='initialview01'>1ukm</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ukm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ukm OCA], [http://www.ebi.ac.uk/pdbsum/1ukm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ukm RCSB]</span> | ||
}} | }} | ||
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[[Category: Morita, T.]] | [[Category: Morita, T.]] | ||
[[Category: Okuda, D.]] | [[Category: Okuda, D.]] | ||
- | [[Category: CL]] | ||
- | [[Category: GOL]] | ||
- | [[Category: NAG]] | ||
[[Category: c-type lectin]] | [[Category: c-type lectin]] | ||
[[Category: domain swapping]] | [[Category: domain swapping]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:11:33 2008'' |
Revision as of 21:11, 30 March 2008
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, resolution 1.90Å | |||||||
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Ligands: | , , | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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
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