1NL2

BOVINE PROTHROMBIN FRAGMENT 1 IN COMPLEX WITH CALCIUM AND LYSOPHOSPHOTIDYLSERINE

Summary for 1NL2

• Entry DOI: 10.2210/pdb1nl2/pdb
• Descriptor: Prothrombin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: hydrolase
• Biological source: Bos taurus (cattle)
• Total number of polymer chains: 1
• Total formula weight: 18375.37

Authors

Huang, M.,Huang, G.,Furie, B.,Seaton, B.,Furie, B.C. (deposition date: 2003-01-06, release date: 2003-09-16, Last modification date: 2023-11-15)

Primary citation

Huang, M.,Rigby, A.C.,Morelli, X.,Grant, M.A.,Huang, G.,Furie, B.,Seaton, B.,Furie, B.C.
Structural basis of membrane binding by Gla domains of vitamin K-dependent proteins.
Nat.Struct.Biol., 10:751-756, 2003

PubMed Abstract: 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.

PubMed: 12923575
DOI: 10.1038/nsb971

Experimental method

X-RAY DIFFRACTION (2.3 Å)