3fib

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:3fib.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:3fib.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3fib| PDB=3fib | SCENE= }}
{{STRUCTURE_3fib| PDB=3fib | SCENE= }}
-
'''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'''
+
===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===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9207064}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9207064 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9207064}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Fibrin polymerization]]
[[Category: Fibrin polymerization]]
[[Category: Fibrinogen]]
[[Category: Fibrinogen]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:01:44 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:20:50 2008''

Revision as of 20:20, 27 July 2008

Image:3fib.png

Template:STRUCTURE 3fib

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

Template:ABSTRACT PUBMED 9207064

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

Page seeded by OCA on Sun Jul 27 23:20:50 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3fib"
Personal tools