Source:http://linkedlifedata.com/resource/pubmed/id/12356313
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
40
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pubmed:dateCreated |
2002-10-1
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pubmed:databankReference | |
pubmed:abstractText |
We report two crystal structures, each at a resolution of 2.8 A, of recombinant human fibrinogen fragment D (rfD) in the absence and presence of peptide ligands. The bound ligands, Gly-Pro-Arg-Pro-amide and Gly-His-Arg-Pro-amide, mimic the interactions of the thrombin exposed polymerization sites, "A" and "B", respectively. This report is the first to describe the structure of fragment D in the presence of both peptide ligands. The structures reveal that recombinant fibrinogen is nearly identical to the plasma protein but with minor changes, like the addition of a proximal fucose to the carbohydrate linked to residue betaGln364, and slightly different relative positions of the beta- and gamma-modules. Of major interest in our structures is that a previously identified calcium site in plasma fibrinogen is absent when Gly-His-Arg-Pro-amide is bound. The peptide-dependent loss of this calcium site may have significant biological implications that are further discussed. These structures provide a foundation for the detailed structural analysis of variant recombinant fibrinogens that were used to identify critical functional residues within fragment D.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrates,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrin Fibrinogen Degradation...,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/fibrinogen D fragment,
http://linkedlifedata.com/resource/pubmed/chemical/glycyl-histidyl-arginyl-proline,
http://linkedlifedata.com/resource/pubmed/chemical/glycyl-prolyl-arginyl-proline
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
41
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12124-32
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12356313-Animals,
pubmed-meshheading:12356313-Binding Sites,
pubmed-meshheading:12356313-CHO Cells,
pubmed-meshheading:12356313-Calcium,
pubmed-meshheading:12356313-Carbohydrates,
pubmed-meshheading:12356313-Cricetinae,
pubmed-meshheading:12356313-Crystallography, X-Ray,
pubmed-meshheading:12356313-Fibrin Fibrinogen Degradation Products,
pubmed-meshheading:12356313-Humans,
pubmed-meshheading:12356313-Ligands,
pubmed-meshheading:12356313-Oligopeptides,
pubmed-meshheading:12356313-Protein Structure, Tertiary
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pubmed:year |
2002
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pubmed:articleTitle |
2.8 A crystal structures of recombinant fibrinogen fragment D with and without two peptide ligands: GHRP binding to the "b" site disrupts its nearby calcium-binding site.
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pubmed:affiliation |
Department of Chemistry, University of North Carolina, Chapel Hill, NC 27599, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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