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1fzd
From Proteopedia
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STRUCTURE OF RECOMBINANT ALPHAEC DOMAIN FROM HUMAN FIBRINOGEN-420
Contents |
Overview
The crystal structure of a recombinant alphaEC domain from human fibrinogen-420 has been determined at a resolution of 2.1 A. The protein, which corresponds to the carboxyl domain of the alphaE chain, was expressed in and purified from Pichia pastoris cells. Felicitously, during crystallization an amino-terminal segment was removed, apparently by a contaminating protease, allowing the 201-residue remaining parent body to crystallize. An x-ray structure was determined by molecular replacement. The electron density was clearly defined, partly as a result of averaging made possible by there being eight molecules in the asymmetric unit related by noncrystallographic symmetry (P1 space group). Virtually all of an asparagine-linked sugar cluster is present. Comparison with structures of the beta- and gamma-chain carboxyl domains of human fibrinogen revealed that the binding cleft is essentially neutral and should not bind Gly-Pro-Arg or Gly-His-Arg peptides of the sort bound by those other domains. Nonetheless, the cleft is clearly evident, and the possibility of binding a carbohydrate ligand like sialic acid has been considered.
Disease
Known diseases associated with this structure: Afibrinogenemia, congenital OMIM:[134820], Amyloidosis, hereditary renal OMIM:[134820], Dysfibrinogenemia, alpha type, causing bleeding diathesis OMIM:[134820], Dysfibrinogenemia, alpha type, causing recurrent thrombosis OMIM:[134820]
About this Structure
1FZD is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of a recombinant alphaEC domain from human fibrinogen-420., Spraggon G, Applegate D, Everse SJ, Zhang JZ, Veerapandian L, Redman C, Doolittle RF, Grieninger G, Proc Natl Acad Sci U S A. 1998 Aug 4;95(16):9099-104. PMID:9689040
Page seeded by OCA on Thu Feb 21 12:44:19 2008
