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PDBsum entry 1bar
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Growth factor
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PDB id
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1bar
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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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Three-Dimensional structures of acidic and basic fibroblast growth factors.
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Authors
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X.Zhu,
H.Komiya,
A.Chirino,
S.Faham,
G.M.Fox,
T.Arakawa,
B.T.Hsu,
D.C.Rees.
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Ref.
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Science, 1991,
251,
90-93.
[DOI no: ]
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PubMed id
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Abstract
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Members of the fibroblast growth factor (FGF) family of proteins stimulate the
proliferation and differentiation of a variety of cell types through
receptor-mediated pathways. The three-dimensional structures of two members of
this family, bovine acidic FGF and human basic FGF, have been
crystallographically determined. These structures contain 12 antiparallel beta
strands organized into a folding pattern with approximate threefold internal
symmetry. Topologically equivalent folds have been previously observed for
soybean trypsin inhibitor and interleukins-1 beta and -1 alpha. The locations of
sequences implicated in receptor and heparin binding by FGF are presented. These
sites include beta-sheet strand 10, which is adjacent to the site of an extended
sequence insertion in several oncogene proteins of the FGF family, and which
shows sequence conservation among the FGF family and interleukin-1 beta.
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