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PDBsum entry 1bld
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Growth factor
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PDB id
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1bld
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References listed in PDB file
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Key reference
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Title
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High-Resolution solution structure of basic fibroblast growth factor determined by multidimensional heteronuclear magnetic resonance spectroscopy.
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Authors
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F.J.Moy,
A.P.Seddon,
P.Böhlen,
R.Powers.
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Ref.
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Biochemistry, 1996,
35,
13552-13561.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
95%.
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Abstract
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The high-resolution solution structure of recombinant human basic fibroblast
growth factor (FGF-2), a protein of 17.2 kDa that exhibits a variety of
functions related to cell growth and differentiation, has been determined using
three-dimensional heteronuclear NMR spectroscopy. A total of 30 structures were
calculated by means of hybrid distance geometry--simulated annealing using a
total of 2865 experimental NMR restraints, consisting of 2486 approximate
inteproton distance restraints, 50 distance restraints for 25 backbone hydrogen
bonds, and 329 torsion angle restraints. The atomic rms distribution about the
mean coordinate positions for the 30 structures for residues 29-152 is 0.43 +/-
0.03 A for the backbone atoms, 0.83 +/- 0.05 A for all atoms, and 0.51 +/- 0.04
A for all atoms excluding disordered side chains. The overall structure of FGF-2
consists of 11 extended antiparallel beta-strands arranged in three groups of
three or four strands connected by tight turns and loop regions creating a
pseudo-3-fold symmetry. Two strands from each group come together to form a
beta-sheet barrel of six antiparallel beta-strands. A helix-like structure was
observed for residues 131-136, which is part of the heparin binding site
(residues 128-138). The discovery of the helix-like region in the primary
heparin binding site instead of the beta-strand conformation described in the
X-ray structures may have important implications in understanding the nature of
heparin--FGF-2 interactions. A total of seven tightly bound water molecules were
found in the FGF-2 structure, two of which are located in the heparin binding
site. The first 28 N-terminal residues appear to be disordered, which is
consistent with previous X-ray structures. A best fit superposition of the NMR
structure of FGF-2 with the 1.9 A resolution X-ray structure by Zhu et al.
(1991) yields a backbone atomic rms difference of 0.94 A, indicative of a close
similarity between the NMR and X-ray structures.
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Secondary reference #1
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Title
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1h, 15n, 13c and 13co assignments and secondary structure determination of basic fibroblast growth factor using 3d heteronuclear nmr spectroscopy.
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Authors
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F.J.Moy,
A.P.Seddon,
E.B.Campbell,
P.Böhlen,
R.Powers.
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Ref.
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J Biomol Nmr, 1995,
6,
245-254.
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PubMed id
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