1RF1

Crystal Structure of Fragment D of gammaE132A Fibrinogen with the Peptide Ligand Gly-His-Arg-Pro-amide

Summary for 1RF1

• Entry DOI: 10.2210/pdb1rf1/pdb
• Related: 1FZC 1FZG 1LT9 1LTJ 1RE3 1RE4 1RF0
• Descriptor: Fibrinogen alpha/alpha-E chain, Fibrinogen beta chain, Fibrinogen gamma chain, ... (7 entities in total)
• Functional Keywords: blood coagulation, fibrinogen, fibrinogen fragment d, recombinant fibrinogen fragment d, fragment d of gammae132a, fibrinogen with ghrp-amide, blood clotting
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 10
• Total formula weight: 160865.89

Authors

Kostelansky, M.S.,Gorkun, O.V.,Lord, S.T. (deposition date: 2003-11-07, release date: 2004-03-16, Last modification date: 2024-11-20)

Primary citation

Kostelansky, M.S.,Lounes, K.C.,Ping, L.F.,Dickerson, S.K.,Gorkun, O.V.,Lord, S.T.
Calcium-Binding Site beta2, Adjacent to the "b" Polymerization Site, Modulates Lateral Aggregation of Protofibrils during Fibrin Polymerization.
Biochemistry, 43:2475-2483, 2004

PubMed Abstract: Structural analysis of recombinant fibrinogen fragment D revealed that the calcium-binding site (beta2-site) composed of residues BbetaAsp261, BbetaAsp398, BbetaGly263, and gammaGlu132 is modulated by the "B:b" interaction. To determine the beta2-site's role in polymerization, we engineered variant fibrinogen gammaE132A in which calcium binding to the beta2-site was disrupted by replacing glutamic acid at gamma132 with alanine. We compared polymerization of gammaE132A to normal fibrinogen as a function of calcium concentration. Polymerization of gammaE132A at concentrations of calcium PubMed: 14992585
DOI: 10.1021/bi0359978

Experimental method

X-RAY DIFFRACTION (2.53 Å)