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PDBsum entry 1fzc
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Blood coagulation
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PDB id
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1fzc
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Contents |
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74 a.a.
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308 a.a.
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301 a.a.
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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 fragment double-D from human fibrin with two different bound ligands.
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Authors
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S.J.Everse,
G.Spraggon,
L.Veerapandian,
M.Riley,
R.F.Doolittle.
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Ref.
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Biochemistry, 1998,
37,
8637-8642.
[DOI no: ]
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PubMed id
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Abstract
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Factor XIII-cross-linked fragment D (double-D) from human fibrin was
crystallized in the presence of two different peptide ligands and the X-ray
structure determined at 2.3 A. The peptide Gly-Pro-Arg-Pro-amide, which is an
analogue of the knob exposed by the thrombin-catalyzed removal of fibrinopeptide
A, was found to reside in the gamma-chain holes, and the peptide
Gly-His-Arg-Pro-amide, which corresponds to the beta-chain knob, was found in
the homologous beta-chain holes. The structure shows for the first time that the
beta-chain knob does indeed bind to a homologous hole on the beta-chain. The
gamma- and beta-chain holes are structurally very similar, and it is remarkable
they are able to distinguish between these two peptides that differ by a single
amino acid. Additionally, we have found that the beta-chain domain, like its
gamma-chain counterpart, binds calcium.
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Secondary reference #1
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Title
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Crystal structures of fragment d from human fibrinogen and its crosslinked counterpart from fibrin.
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Authors
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G.Spraggon,
S.J.Everse,
R.F.Doolittle.
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Ref.
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Nature, 1997,
389,
455-462.
[DOI no: ]
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PubMed id
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Figure 4.
Figure 4 a, Topology of  -chain
(green) and  -chain
(red) C-terminal domains. The first residue in each segment of
secondary structure is numbered. b, Stereo depiction of
superposed C  backbone
structures from globular portions of -chains
(green) and -chains
(red); the numbers on the strands and letters on the helices
correspond to the secondary structure designations in Fig. 4. c,
GRASP representation of binding cavities of -chains
(left) and -chains
(right) showing charge distribution; red, negatively charged;
blue, positively charged^47. Domains have been reorientated to
show equivalent projections.
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Figure 5.
Figure 5 a, Topology of -chain
(green) and -chain
(red) C-terminal domains. The first residue in each segment of
secondary structure is numbered. b, Stereo depiction of
superposed C backbone
structures from globular portions of -chains
(green) and -chains
(red); the numbers on the strands and letters on the helices
correspond to the secondary structure designations in Fig. 4. c,
GRASP representation of binding cavities of -chains
(left) and -chains
(right) showing charge distribution; red, negatively charged;
blue, positively charged^47. Domains have been reorientated to
show equivalent projections.
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The above figures are
reproduced from the cited reference
with permission from Macmillan Publishers Ltd
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Secondary reference #2
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Title
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Erratum. Crystal structures of fragment d from human fibrinogen and its crosslinked counterpart from fibrin
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Authors
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G.Spraggon,
S.J.Everse,
R.F.Doolittle.
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Ref.
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nature, 1997,
390,
315.
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