2bfh
From Proteopedia
(New page: 200px<br /> <applet load="2bfh" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bfh, resolution 2.5Å" /> '''CRYSTAL STRUCTURE OF...) |
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caption="2bfh, resolution 2.5Å" /> | caption="2bfh, resolution 2.5Å" /> | ||
'''CRYSTAL STRUCTURE OF BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BFH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2BFH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: growth factor]] | [[Category: growth factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:16:14 2008'' |
Revision as of 15:16, 15 February 2008
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CRYSTAL STRUCTURE OF BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION
Contents |
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
2BFH 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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