1v7p

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(New page: 200px<br /> <applet load="1v7p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v7p, resolution 1.90&Aring;" /> '''Structure of EMS16-...)
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<applet load="1v7p" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1v7p, resolution 1.90&Aring;" />
caption="1v7p, resolution 1.90&Aring;" />
'''Structure of EMS16-alpha2-I domain complex'''<br />
'''Structure of EMS16-alpha2-I domain complex'''<br />
==Overview==
==Overview==
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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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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.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1V7P is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Echis_multisquamatus Echis multisquamatus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG, PO4, MN and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V7P OCA].
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1V7P is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Echis_multisquamatus Echis multisquamatus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V7P OCA].
==Reference==
==Reference==
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[[Category: snake venom]]
[[Category: snake venom]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:42:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:32:20 2008''

Revision as of 13:32, 21 February 2008


1v7p, resolution 1.90Å

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Structure of EMS16-alpha2-I domain complex

Contents

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.

Disease

Known diseases associated with this structure: Glycoprotein Ia deficiency (1) OMIM:[192974], Neonatal alloimmune thrombocytopenia OMIM:[192974]

About this Structure

1V7P is a Protein complex structure of sequences from Echis multisquamatus and Homo sapiens with , , and as ligands. 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

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