1sdd

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(New page: 200px<br /><applet load="1sdd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sdd, resolution 2.8&Aring;" /> '''Crystal Structure of ...)
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[[Image:1sdd.gif|left|200px]]<br /><applet load="1sdd" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1sdd, resolution 2.8&Aring;" />
'''Crystal Structure of Bovine Factor Vai'''<br />
'''Crystal Structure of Bovine Factor Vai'''<br />
==Overview==
==Overview==
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In vertebrate hemostasis, factor Va serves as the cofactor in the, prothrombinase complex that results in a 300,000-fold increase in the rate, of thrombin generation compared with factor Xa alone. Structurally, little, is known about the mechanism by which factor Va alters catalysis within, this complex. Here, we report a crystal structure of protein C inactivated, factor Va (A1.A3-C1-C2) that depicts a previously uncharacterized domain, arrangement. This orientation has implications for binding to membranes, essential for function. A high-affinity calcium-binding site and a, copper-binding site have both been identified. Surprisingly, neither shows, a direct involvement in chain association. This structure represents the, largest physiologically relevant fragment of factor Va solved to date and, provides a new scaffold for the future generation of models of coagulation, cofactors.
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In vertebrate hemostasis, factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation compared with factor Xa alone. Structurally, little is known about the mechanism by which factor Va alters catalysis within this complex. Here, we report a crystal structure of protein C inactivated factor Va (A1.A3-C1-C2) that depicts a previously uncharacterized domain arrangement. This orientation has implications for binding to membranes essential for function. A high-affinity calcium-binding site and a copper-binding site have both been identified. Surprisingly, neither shows a direct involvement in chain association. This structure represents the largest physiologically relevant fragment of factor Va solved to date and provides a new scaffold for the future generation of models of coagulation cofactors.
==About this Structure==
==About this Structure==
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1SDD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with NAG, NDG, CU and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SDD OCA].
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1SDD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=NDG:'>NDG</scene>, <scene name='pdbligand=CU:'>CU</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SDD OCA].
==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Adams, T.E.]]
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[[Category: Adams, T E.]]
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[[Category: Everse, S.J.]]
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[[Category: Everse, S J.]]
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[[Category: Hockin, M.F.]]
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[[Category: Hockin, M F.]]
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[[Category: Mann, K.G.]]
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[[Category: Mann, K G.]]
[[Category: CA]]
[[Category: CA]]
[[Category: CU]]
[[Category: CU]]
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[[Category: copper-binding protein]]
[[Category: copper-binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:17:52 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:00:23 2008''

Revision as of 13:00, 21 February 2008


1sdd, resolution 2.8Å

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Crystal Structure of Bovine Factor Vai

Overview

In vertebrate hemostasis, factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation compared with factor Xa alone. Structurally, little is known about the mechanism by which factor Va alters catalysis within this complex. Here, we report a crystal structure of protein C inactivated factor Va (A1.A3-C1-C2) that depicts a previously uncharacterized domain arrangement. This orientation has implications for binding to membranes essential for function. A high-affinity calcium-binding site and a copper-binding site have both been identified. Surprisingly, neither shows a direct involvement in chain association. This structure represents the largest physiologically relevant fragment of factor Va solved to date and provides a new scaffold for the future generation of models of coagulation cofactors.

About this Structure

1SDD is a Protein complex structure of sequences from Bos taurus with , , and as ligands. Full crystallographic information is available from OCA.

Reference

The crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function., Adams TE, Hockin MF, Mann KG, Everse SJ, Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8918-23. Epub 2004 Jun 7. PMID:15184653

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