1fze: Difference between revisions

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[[Image:1fze.gif|left|200px]]
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[[Image:1fze.png|left|200px]]


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{{STRUCTURE_1fze|  PDB=1fze  |  SCENE=  }}  
{{STRUCTURE_1fze|  PDB=1fze  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN'''
===CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN===




==Overview==
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The structure of fragment double-D from human fibrin has been solved in the presence and absence of the peptide ligands that simulate the two knobs exposed by the removal of fibrinopeptides A and B, respectively. All told, six crystal structures have been determined, three of which are reported here for the first time: namely, fragments D and double-D with the peptide GHRPam alone and double-D in the absence of any peptide ligand. Comparison of the structures has revealed a series of conformational changes that are brought about by the various knob-hole interactions. Of greatest interest is a moveable "flap" of two negatively charged amino acids (Glubeta397 and Aspbeta398) whose side chains are pinned back to the coiled coil with a calcium atom bridge until GHRPam occupies the beta-chain pocket. Additionally, in the absence of the peptide ligand GPRPam, GHRPam binds to the gamma-chain pocket, a new calcium-binding site being formed concomitantly.
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{{ABSTRACT_PUBMED_10074346}}


==About this Structure==
==About this Structure==
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[[Category: Plasma]]
[[Category: Plasma]]
[[Category: Platelet]]
[[Category: Platelet]]
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Revision as of 04:10, 1 July 2008

File:1fze.png

Template:STRUCTURE 1fze

CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRINCRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN

Template:ABSTRACT PUBMED 10074346

About this StructureAbout this Structure

1FZE is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide., Everse SJ, Spraggon G, Veerapandian L, Doolittle RF, Biochemistry. 1999 Mar 9;38(10):2941-6. PMID:10074346

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