1nl2

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spinqualitylabelsall models 1nl2, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

BOVINE PROTHROMBIN FRAGMENT 1 IN COMPLEX WITH CALCIUM AND LYSOPHOSPHOTIDYLSERINE

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

1NL2 is a Single protein structure of sequence from Bos taurus with NAG, CA, CL and LPS as ligands. Active as Thrombin, with EC number 3.4.21.5 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

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