1bfg: Difference between revisions
New page: left|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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[[Image:1bfg.gif|left|200px]]<br /> | [[Image:1bfg.gif|left|200px]]<br /><applet load="1bfg" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1bfg, resolution 1.6Å" /> | caption="1bfg, resolution 1.6Å" /> | ||
'''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 /> | ||
==Overview== | ==Overview== | ||
We have determined the crystal structures of two types of human basic | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1BFG 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:// | 1BFG 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=1BFG OCA]. | ||
==Reference== | ==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 | Crystal structure of basic fibroblast growth factor at 1.6 A resolution., Ago H, Kitagawa Y, Fujishima A, Matsuura Y, Katsube Y, J Biochem. 1991 Sep;110(3):360-3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1769963 1769963] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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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 Thu Feb 21 11:54:45 2008'' | ||
Revision as of 12:54, 21 February 2008
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CRYSTAL STRUCTURE OF BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION
OverviewOverview
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.
DiseaseDisease
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 StructureAbout this Structure
1BFG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of basic fibroblast growth factor at 1.6 A resolution., Ago H, Kitagawa Y, Fujishima A, Matsuura Y, Katsube Y, J Biochem. 1991 Sep;110(3):360-3. PMID:1769963
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