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PDBsum entry 1fzd
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Blood coagulation
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PDB id
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1fzd
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of a recombinant alphaec domain from human fibrinogen-420.
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Authors
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G.Spraggon,
D.Applegate,
S.J.Everse,
J.Z.Zhang,
L.Veerapandian,
C.Redman,
R.F.Doolittle,
G.Grieninger.
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Ref.
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Proc Natl Acad Sci U S A, 1998,
95,
9099-9104.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 1.
Fig. 1. Crystal of r  [E]C domain
used for x-ray diffraction study. The crystal measured  0.5 mm on its
longest edge.
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Figure 4.
Fig. 4. GRASP (35) depictions of [E]C (Left)
and  C (Right)
domains showing equivalent projections with binding clefts. The
ball and stick model is liganded Gly-Pro-Arg-Pro-amide. Note
lack of negative charge (red) within the binding site of the
[E]C chains.
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