1v7p
From Proteopedia
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|PDB= 1v7p |SIZE=350|CAPTION= <scene name='initialview01'>1v7p</scene>, resolution 1.90Å | |PDB= 1v7p |SIZE=350|CAPTION= <scene name='initialview01'>1v7p</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ukm|1UKM]], [[1aox|1AOX]], [[1dzi|1DZI]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v7p OCA], [http://www.ebi.ac.uk/pdbsum/1v7p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v7p RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
Snake venoms contain a number of heterodimeric C-type lectin-like proteins (CLPs) that interact specifically with components of the haemostatic system. EMS16 from the venom of Echis multisquamatus binds to the collagen receptor, integrin alpha2beta1, also known as glycoprotein (GP) Ia/IIa, and specifically inhibits collagen binding. Here we report the crystal structure of EMS16 in complex with recombinant integrin alpha2-I domain that plays a central role in collagen binding. The structure of the complex at 1.9 Angstrom resolution reveals that the collagen-binding site of the alpha2-I domain is covered completely by the bound EMS16. This blockage by EMS16 appears to spatially inhibit collagen binding to the alpha2-I domain. The bound alpha2-I domain adopts a closed conformation, which is seen in the absence of ligand, suggesting that EMS16 stabilizes a closed conformation corresponding to the less active structure of the alpha2-I domain. EMS16 does not directly bind to the manganese ion and residues of the metal ion-dependent adhesion site (MIDAS) of the alpha2-I domain, suggesting that EMS16 may have the potential to bind specifically to the alpha2-I domain in a metal ion-independent fashion. | Snake venoms contain a number of heterodimeric C-type lectin-like proteins (CLPs) that interact specifically with components of the haemostatic system. EMS16 from the venom of Echis multisquamatus binds to the collagen receptor, integrin alpha2beta1, also known as glycoprotein (GP) Ia/IIa, and specifically inhibits collagen binding. Here we report the crystal structure of EMS16 in complex with recombinant integrin alpha2-I domain that plays a central role in collagen binding. The structure of the complex at 1.9 Angstrom resolution reveals that the collagen-binding site of the alpha2-I domain is covered completely by the bound EMS16. This blockage by EMS16 appears to spatially inhibit collagen binding to the alpha2-I domain. The bound alpha2-I domain adopts a closed conformation, which is seen in the absence of ligand, suggesting that EMS16 stabilizes a closed conformation corresponding to the less active structure of the alpha2-I domain. EMS16 does not directly bind to the manganese ion and residues of the metal ion-dependent adhesion site (MIDAS) of the alpha2-I domain, suggesting that EMS16 may have the potential to bind specifically to the alpha2-I domain in a metal ion-independent fashion. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Glycoprotein Ia deficiency (1) OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=192974 192974]], Neonatal alloimmune thrombocytopenia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=192974 192974]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Morita, T.]] | [[Category: Morita, T.]] | ||
[[Category: Okuda, D.]] | [[Category: Okuda, D.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: MN]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: PO4]] | ||
[[Category: antagonist]] | [[Category: antagonist]] | ||
[[Category: c-type lectin]] | [[Category: c-type lectin]] | ||
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[[Category: snake venom]] | [[Category: snake venom]] | ||
| - | ''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 00:20:34 2008'' |
Revision as of 21:20, 30 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Related: | 1UKM, 1AOX, 1DZI
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of EMS16-alpha2-I domain complex
Overview
Snake venoms contain a number of heterodimeric C-type lectin-like proteins (CLPs) that interact specifically with components of the haemostatic system. EMS16 from the venom of Echis multisquamatus binds to the collagen receptor, integrin alpha2beta1, also known as glycoprotein (GP) Ia/IIa, and specifically inhibits collagen binding. Here we report the crystal structure of EMS16 in complex with recombinant integrin alpha2-I domain that plays a central role in collagen binding. The structure of the complex at 1.9 Angstrom resolution reveals that the collagen-binding site of the alpha2-I domain is covered completely by the bound EMS16. This blockage by EMS16 appears to spatially inhibit collagen binding to the alpha2-I domain. The bound alpha2-I domain adopts a closed conformation, which is seen in the absence of ligand, suggesting that EMS16 stabilizes a closed conformation corresponding to the less active structure of the alpha2-I domain. EMS16 does not directly bind to the manganese ion and residues of the metal ion-dependent adhesion site (MIDAS) of the alpha2-I domain, suggesting that EMS16 may have the potential to bind specifically to the alpha2-I domain in a metal ion-independent fashion.
About this Structure
1V7P is a Protein complex structure of sequences from Echis multisquamatus and Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of EMS16 in complex with the integrin alpha2-I domain., Horii K, Okuda D, Morita T, Mizuno H, J Mol Biol. 2004 Aug 6;341(2):519-27. PMID:15276841
Page seeded by OCA on Mon Mar 31 00:20:34 2008
