1fzg

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[[Image:1fzg.gif|left|200px]]
[[Image:1fzg.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fzg OCA], [http://www.ebi.ac.uk/pdbsum/1fzg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fzg RCSB]</span>
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'''CRYSTAL STRUCTURE OF FRAGMENT D FROM HUMAN FIBRINOGEN WITH THE PEPTIDE LIGAND GLY-HIS-ARG-PRO-AMIDE'''
'''CRYSTAL STRUCTURE OF FRAGMENT D FROM HUMAN FIBRINOGEN WITH THE PEPTIDE LIGAND GLY-HIS-ARG-PRO-AMIDE'''
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[[Category: Spraggon, G.]]
[[Category: Spraggon, G.]]
[[Category: Veerapandian, L.]]
[[Category: Veerapandian, L.]]
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[[Category: blood coagulation]]
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[[Category: Blood coagulation]]
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[[Category: fibrin]]
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[[Category: Fibrin]]
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[[Category: fibrinogen]]
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[[Category: Fibrinogen]]
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[[Category: plasma]]
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[[Category: Plasma]]
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[[Category: platelet]]
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[[Category: Platelet]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:56:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:33:16 2008''
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Revision as of 13:56, 2 May 2008

Template:STRUCTURE 1fzg

CRYSTAL STRUCTURE OF FRAGMENT D FROM HUMAN FIBRINOGEN WITH THE PEPTIDE LIGAND GLY-HIS-ARG-PRO-AMIDE


Overview

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.

About this Structure

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

Reference

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 Page seeded by OCA on Fri May 2 16:56:23 2008

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