1nl1

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|PDB= 1nl1 |SIZE=350|CAPTION= <scene name='initialview01'>1nl1</scene>, resolution 1.90&Aring;
|PDB= 1nl1 |SIZE=350|CAPTION= <scene name='initialview01'>1nl1</scene>, resolution 1.90&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CGU:GAMMA-CARBOXY-GLUTAMIC+ACID'>CGU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Thrombin Thrombin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.5 3.4.21.5]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Thrombin Thrombin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.5 3.4.21.5] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[2pf2|2pf2]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nl1 OCA], [http://www.ebi.ac.uk/pdbsum/1nl1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nl1 RCSB]</span>
}}
}}
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[[Category: Huang, M.]]
[[Category: Huang, M.]]
[[Category: Seaton, B.]]
[[Category: Seaton, B.]]
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[[Category: CA]]
 
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[[Category: NAG]]
 
[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:58:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:31:48 2008''

Revision as of 19:31, 30 March 2008

Image:1nl1.gif


PDB ID 1nl1

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands: , ,
Activity: Thrombin, with EC number 3.4.21.5
Related: 2pf2


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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