2fib: Difference between revisions

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[[Image:2fib.gif|left|200px]]
[[Image:2fib.gif|left|200px]]


{{Structure
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|PDB= 2fib |SIZE=350|CAPTION= <scene name='initialview01'>2fib</scene>, resolution 2.01&Aring;
The line below this paragraph, containing "STRUCTURE_2fib", creates the "Structure Box" on the page.
|SITE=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|GENE= HUMAN FIBRINOGEN GAMMA CHAIN CDNA ENCODING VAL 143 - VAL 411 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
{{STRUCTURE_2fib| PDB=2fib  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fib OCA], [http://www.ebi.ac.uk/pdbsum/2fib PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fib RCSB]</span>
}}


'''RECOMBINANT HUMAN GAMMA-FIBRINOGEN CARBOXYL TERMINAL FRAGMENT (RESIDUES 143-411) COMPLEXED TO THE PEPTIDE GLY-PRO-ARG-PRO AT PH 6.0'''
'''RECOMBINANT HUMAN GAMMA-FIBRINOGEN CARBOXYL TERMINAL FRAGMENT (RESIDUES 143-411) COMPLEXED TO THE PEPTIDE GLY-PRO-ARG-PRO AT PH 6.0'''
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[[Category: Pratt, K P.]]
[[Category: Pratt, K P.]]
[[Category: Stenkamp, R E.]]
[[Category: Stenkamp, R E.]]
[[Category: blood coagulation]]
[[Category: Blood coagulation]]
[[Category: complex (blood coagulation/peptide)]]
[[Category: Fibrin polymerization]]
[[Category: fibrin polymerization]]
[[Category: Fibrinogen]]
[[Category: fibrinogen]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:55:57 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:03:13 2008''

Revision as of 03:55, 4 May 2008

File:2fib.gif

Template:STRUCTURE 2fib

RECOMBINANT HUMAN GAMMA-FIBRINOGEN CARBOXYL TERMINAL FRAGMENT (RESIDUES 143-411) COMPLEXED TO THE PEPTIDE GLY-PRO-ARG-PRO AT PH 6.0


OverviewOverview

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.

About this StructureAbout this Structure

2FIB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Sun May 4 03:55:57 2008

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