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Structural basis of membrane binding by Gla domains of vitamin K-dependent proteins.
- Source :
-
Nature Structural Biology . Sep2003, Vol. 10 Issue 9, p751-756. 6p. - Publication Year :
- 2003
-
Abstract
- In a calcium-dependent interaction critical for blood coagulation, vitamin K-dependent blood coagulation proteins bind cell membranes containing phosphatidylserine via ?-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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 10728368
- Volume :
- 10
- Issue :
- 9
- Database :
- Academic Search Index
- Journal :
- Nature Structural Biology
- Publication Type :
- Academic Journal
- Accession number :
- 10659934
- Full Text :
- https://doi.org/10.1038/nsb971