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1nl1
From Proteopedia
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'''BOVINE PROTHROMBIN FRAGMENT 1 IN COMPLEX WITH CALCIUM ION''' | '''BOVINE PROTHROMBIN FRAGMENT 1 IN COMPLEX WITH CALCIUM ION''' | ||
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[[Category: Huang, M.]] | [[Category: Huang, M.]] | ||
[[Category: Seaton, B.]] | [[Category: Seaton, B.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:39:36 2008'' | |
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Revision as of 23:39, 2 May 2008
BOVINE PROTHROMBIN FRAGMENT 1 IN COMPLEX WITH CALCIUM ION
Overview
In a calcium-dependent interaction critical for blood coagulation, vitamin K-dependent blood coagulation proteins bind cell membranes containing phosphatidylserine via gamma-carboxyglutamic acid-rich (Gla) domains. Gla domain-mediated protein-membrane interaction is required for generation of thrombin, the terminal enzyme in the coagulation cascade, on a physiologic time scale. We determined by X-ray crystallography and NMR spectroscopy the lysophosphatidylserine-binding site in the bovine prothrombin Gla domain. The serine head group binds Gla domain-bound calcium ions and Gla residues 17 and 21, fixed elements of the Gla domain fold, predicting the structural basis for phosphatidylserine specificity among Gla domains. Gla domains provide a unique mechanism for protein-phospholipid membrane interaction. Increasingly Gla domains are being identified in proteins unrelated to blood coagulation. Thus, this membrane-binding mechanism may be important in other physiologic processes.
About this Structure
1NL1 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Structural basis of membrane binding by Gla domains of vitamin K-dependent proteins., Huang M, Rigby AC, Morelli X, Grant MA, Huang G, Furie B, Seaton B, Furie BC, Nat Struct Biol. 2003 Sep;10(9):751-6. Epub 2003 Aug 17. PMID:12923575 Page seeded by OCA on Sat May 3 02:39:36 2008
Categories: Bos taurus | Single protein | Thrombin | Furie, B. | Furie, B C. | Huang, G. | Huang, M. | Seaton, B. | Hydrolase
