1bfg
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(New page: 200px<br /> <applet load="1bfg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bfg, resolution 1.6Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 14:02, 12 November 2007
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CRYSTAL STRUCTURE OF BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION
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Overview
We have determined the crystal structures of two types of human basic, fibroblast growth factor, the serine analogue and the wild-type, at 1.6, and 2.5 A resolution, respectively. Two good heavy atom derivatives were, found and used for multiple isomorphous replacement phasing. The atomic, coordinates were refined using the Hendrickson & Konnert program for, stereochemically restrained refinement against structure factors. The, crystallographic R factors were reduced to 15.3% for the serine analogue, structure and 16.0% for the wild-type structure. The serine analogue and, wild-type structures have been found to be almost identical, the, root-mean-square deviation between the corresponding C alpha atoms being, 0.11 A. Their structures are composed of twelve beta-strands forming a, barrel and three loops. Their molecules have an approximate threefold, internal symmetry and are similar in architecture to that of interleukin-1, beta. A possible heparin-binding site, which comprises five basic, residues, Lys119, Arg120, Lys125, Lys129, and Lys135, has been revealed by, calculating the electrostatic potential energy.
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
1BFG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of basic fibroblast growth factor at 1.6 A resolution., Ago H, Kitagawa Y, Fujishima A, Matsuura Y, Katsube Y, J Biochem (Tokyo). 1991 Sep;110(3):360-3. PMID:1769963
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