1FZD

STRUCTURE OF RECOMBINANT ALPHAEC DOMAIN FROM HUMAN FIBRINOGEN-420

Summary for 1FZD

• Entry DOI: 10.2210/pdb1fzd/pdb
• Descriptor: FIBRINOGEN-420, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: blood coagulation, fibrinogen-420, alphaec domain, fibrinogen related domain, glycosylated protein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P02671
• Total number of polymer chains: 8
• Total formula weight: 189235.60

Authors

Spraggon, G.,Applegate, D.,Everse, S.J.,Zhang, J.-Z.,Veerapandian, L.,Redman, C.,Doolittle, R.F.,Grieninger, G. (deposition date: 1998-06-22, release date: 1998-08-19, Last modification date: 2023-08-09)

Primary citation

Spraggon, G.,Applegate, D.,Everse, S.J.,Zhang, J.Z.,Veerapandian, L.,Redman, C.,Doolittle, R.F.,Grieninger, G.
Crystal structure of a recombinant alphaEC domain from human fibrinogen-420.
Proc.Natl.Acad.Sci.USA, 95:9099-9104, 1998

PubMed Abstract: 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.

PubMed: 9689040
DOI: 10.1073/pnas.95.16.9099

Experimental method

X-RAY DIFFRACTION (2.1 Å)