2h43

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{{STRUCTURE_2h43| PDB=2h43 | SCENE= }}
{{STRUCTURE_2h43| PDB=2h43 | SCENE= }}
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'''Crystal Structure of Human Fragment D Complexed with Ala-His-Arg-Pro-amide'''
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===Crystal Structure of Human Fragment D Complexed with Ala-His-Arg-Pro-amide===
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==Overview==
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The beta-chain amino-terminal sequences of all known mammalian fibrins begin with the sequence Gly-His-Arg-Pro- (GHRP-), but the homologous sequence in chicken fibrin begins with the sequence Ala-His-Arg-Pro- (AHRP-). Nonetheless, chicken fibrinogen binds the synthetic peptide GHRPam, and a previously reported crystal structure has revealed that the binding is in exact conformance with that observed for the human GHRPam-fragment D complex. We now report that human fibrinogen, which is known not to bind APRP, binds the synthetic peptide AHRPam. Moreover, a crystal structure of AHRPam complexed with fragment D from human fibrinogen shows that AHRPam binds exclusively to the beta-chain hole and, unlike GHRPam, not at all to the homologous gamma-chain hole. The difference can be attributed to the methyl group of the alanine residue clashing with a critical carboxyl group in the gammaC hole but being accommodated in the roomier betaC hole where the equivalent carboxyl is situated more flexibly.
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(as it appears on PubMed at http://www.pubmed.gov), where 17115691 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17115691}}
==About this Structure==
==About this Structure==
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[[Category: Fragment d]]
[[Category: Fragment d]]
[[Category: Knob-hole interaction]]
[[Category: Knob-hole interaction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:50:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:40:30 2008''

Revision as of 04:40, 28 July 2008

Template:STRUCTURE 2h43

Crystal Structure of Human Fragment D Complexed with Ala-His-Arg-Pro-amide

Template:ABSTRACT PUBMED 17115691

About this Structure

2H43 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Differences in binding specificity for the homologous gamma- and beta-chain "holes" on fibrinogen: exclusive binding of Ala-His-Arg-Pro-amide by the beta-chain hole., Doolittle RF, Chen A, Pandi L, Biochemistry. 2006 Nov 28;45(47):13962-9. PMID:17115691

Page seeded by OCA on Mon Jul 28 07:40:30 2008

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