1fgk

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[[Image:1fgk.gif|left|200px]]
[[Image:1fgk.gif|left|200px]]
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{{Structure
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|PDB= 1fgk |SIZE=350|CAPTION= <scene name='initialview01'>1fgk</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1fgk", creates the "Structure Box" on the page.
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] </span>
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{{STRUCTURE_1fgk| PDB=1fgk | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgk OCA], [http://www.ebi.ac.uk/pdbsum/1fgk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fgk RCSB]</span>
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'''CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF FIBROBLAST GROWTH FACTOR RECEPTOR 1'''
'''CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF FIBROBLAST GROWTH FACTOR RECEPTOR 1'''
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[[Category: Mohammadi, M.]]
[[Category: Mohammadi, M.]]
[[Category: Schlessinger, J.]]
[[Category: Schlessinger, J.]]
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[[Category: atp-binding]]
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[[Category: Atp-binding]]
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[[Category: phosphorylation]]
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[[Category: Phosphorylation]]
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[[Category: phosphotransferase]]
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[[Category: Phosphotransferase]]
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[[Category: receptor]]
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[[Category: Receptor]]
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[[Category: transferase]]
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[[Category: Transferase]]
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[[Category: tyrosine-protein kinase]]
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[[Category: Tyrosine-protein kinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:18:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:22:26 2008''
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Revision as of 13:18, 2 May 2008

Image:1fgk.gif

Template:STRUCTURE 1fgk

CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF FIBROBLAST GROWTH FACTOR RECEPTOR 1


Overview

The crystal structure of the tyrosine kinase domain of fibroblast growth factor receptor 1 (FGFR1K) has been determined in its unliganded form to 2.0 angstroms resolution and in complex with with an ATP analog to 2.3 angstrosms A resolution. Several features distinguish the structure of FGFR1K from that of the tyrosine kinase domain of the insulin receptor. Residues in the activation loop of FGFR1K appear to interfere with substrate peptide binding but not with ATP binding, revealing a second and perhaps more general autoinhibitory mechanism for receptor tyrosine kinases. In addition, a dimeric form of FGFR1K observed in the crystal structure may provide insights into the molecular mechanisms by which FGF receptors are activated. Finally, the structure provides a basis for rationalizing the effects of kinase mutations in FGF receptors that lead to developmental disorders in nematodes and humans.

About this Structure

1FGK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism., Mohammadi M, Schlessinger J, Hubbard SR, Cell. 1996 Aug 23;86(4):577-87. PMID:8752212 Page seeded by OCA on Fri May 2 16:18:02 2008

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