1bld
From Proteopedia
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BASIC FIBROBLAST GROWTH FACTOR (FGF-2) MUTANT WITH CYS 78 REPLACED BY SER AND CYS 96 REPLACED BY SER, NMR
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Overview
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.
Disease
Known diseases associated with this structure: Hypophosphatemic rickets, autosomal dominant OMIM:[605380], Osteomalacia, tumor-induced OMIM:[605380], Tumoral calcinosis, hyperphosphatemic, familial OMIM:[605380]
About this Structure
1BLD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
High-resolution solution structure of basic fibroblast growth factor determined by multidimensional heteronuclear magnetic resonance spectroscopy., Moy FJ, Seddon AP, Bohlen P, Powers R, Biochemistry. 1996 Oct 22;35(42):13552-61. PMID:8885834
Page seeded by OCA on Mon Nov 12 16:11:27 2007
