3fib
From Proteopedia
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| - | [[Image:3fib.jpg|left|200px]] | + | [[Image:3fib.jpg|left|200px]] |
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| - | '''RECOMBINANT HUMAN GAMMA-FIBRINOGEN CARBOXYL TERMINAL FRAGMENT (RESIDUES 143-411) BOUND TO CALCIUM AT PH 6.0: A FURTHER REFINEMENT OF PDB ENTRY 1FIB, AND DIFFERS FROM 1FIB BY THE MODELLING OF A CIS PEPTIDE BOND BETWEEN RESIDUES K338 AND C339''' | + | {{Structure |
| + | |PDB= 3fib |SIZE=350|CAPTION= <scene name='initialview01'>3fib</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''RECOMBINANT HUMAN GAMMA-FIBRINOGEN CARBOXYL TERMINAL FRAGMENT (RESIDUES 143-411) BOUND TO CALCIUM AT PH 6.0: A FURTHER REFINEMENT OF PDB ENTRY 1FIB, AND DIFFERS FROM 1FIB BY THE MODELLING OF A CIS PEPTIDE BOND BETWEEN RESIDUES K338 AND C339''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 3FIB is a [ | + | 3FIB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FIB OCA]. |
==Reference== | ==Reference== | ||
| - | The primary fibrin polymerization pocket: three-dimensional structure of a 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-Arg-Pro., Pratt KP, Cote HC, Chung DW, Stenkamp RE, Davie EW, Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7176-81. PMID:[http:// | + | The primary fibrin polymerization pocket: three-dimensional structure of a 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-Arg-Pro., Pratt KP, Cote HC, Chung DW, Stenkamp RE, Davie EW, Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7176-81. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9207064 9207064] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: CA]] | [[Category: CA]] | ||
[[Category: blood coagulation]] | [[Category: blood coagulation]] | ||
| - | [[Category: cis peptide | + | [[Category: cis peptide bond]] |
[[Category: fibrin polymerization]] | [[Category: fibrin polymerization]] | ||
[[Category: fibrinogen]] | [[Category: fibrinogen]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:04:48 2008'' |
Revision as of 17:04, 20 March 2008
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| , resolution 2.1Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
RECOMBINANT HUMAN GAMMA-FIBRINOGEN CARBOXYL TERMINAL FRAGMENT (RESIDUES 143-411) BOUND TO CALCIUM AT PH 6.0: A FURTHER REFINEMENT OF PDB ENTRY 1FIB, AND DIFFERS FROM 1FIB BY THE MODELLING OF A CIS PEPTIDE BOND BETWEEN RESIDUES K338 AND C339
Contents |
Overview
After vascular injury, a cascade of serine protease activations leads to the conversion of the soluble fibrinogen molecule into fibrin. The fibrin monomers then polymerize spontaneously and noncovalently to form a fibrin gel. The primary interaction of this polymerization reaction is between the newly exposed N-terminal Gly-Pro-Arg sequence of the alpha chain of one fibrin molecule and the C-terminal region of a gamma chain of an adjacent fibrin(ogen) molecule. In this report, the polymerization pocket has been identified by determining the crystal structure of a 30-kDa C-terminal fragment of the fibrin(ogen) gamma chain complexed with the peptide Gly-Pro-Arg-Pro. This peptide mimics the N terminus of the alpha chain of fibrin. The conformational change in the protein upon binding the peptide is subtle, with electrostatic interactions primarily mediating the association. This is consistent with biophysical experiments carried out over the last 50 years on this fundamental polymerization reaction.
Disease
Known diseases associated with this structure: Dysfibrinogenemia, gamma type OMIM:[134850], Hypofibrinogenemia, gamma type OMIM:[134850], Thrombophilia, dysfibrinogenemic OMIM:[134850]
About this Structure
3FIB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The primary fibrin polymerization pocket: three-dimensional structure of a 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-Arg-Pro., Pratt KP, Cote HC, Chung DW, Stenkamp RE, Davie EW, Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7176-81. PMID:9207064
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