1FZF
CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN WITH THE PEPTIDE LIGAND GLY-HIS-ARG-PRO-AMIDE
Summary for 1FZF
Entry DOI | 10.2210/pdb1fzf/pdb |
Descriptor | FIBRINOGEN, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (6 entities in total) |
Functional Keywords | blood coagulation, plasma, platelet, fibrinogen, fibrin |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 10 |
Total formula weight | 170873.44 |
Authors | Everse, S.J.,Spraggon, G.,Veerapandian, L.,Doolittle, R.F. (deposition date: 1998-12-28, release date: 1999-06-08, Last modification date: 2024-10-30) |
Primary citation | Everse, S.J.,Spraggon, G.,Veerapandian, L.,Doolittle, R.F. Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide. Biochemistry, 38:2941-2946, 1999 Cited by PubMed Abstract: 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. PubMed: 10074346DOI: 10.1021/bi982626w PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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