4tyi
From Proteopedia
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| - | ''' | + | ==Structural analysis of the human Fibroblast Growth Factor Receptor 4== |
| + | <StructureSection load='4tyi' size='340' side='right' caption='[[4tyi]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4tyi]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TYI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TYI FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=38O:4-AMINO-5-FLUORO-3-[5-(4-METHYLPIPERAZIN-1-YL)-1H-BENZIMIDAZOL-2-YL]QUINOLIN-2(1H)-ONE'>38O</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tye|4tye]], [[4tyg|4tyg]], [[4tyj|4tyj]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tyi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tyi RCSB], [http://www.ebi.ac.uk/pdbsum/4tyi PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The family of Fibroblast Growth Factor Receptors (FGFRs) plays an important and well characterized role in a variety of pathological disorders. FGFR4 is involved in myogenesis and muscle regeneration. Mutations affecting the kinase domain of FGFR4 may cause cancer e.g. breast cancer or rhabdomyosarcoma. Whereas FGFRs 1-3 have been structurally characterized, the structure of the FGFR4 kinase domain has not yet been reported. In this study we present four structures of the kinase domain of FGFR4, in its apo-form and in complex with different types of small-molecule inhibitors. The two apo-FGFR4 kinase domain structures show an activation segment similar in conformation to an autoinhibitory segment observed in the hepatocyte growth factor receptor kinase but different from the known structures of other FGFR kinases. The structures of FGFR4 in complex with the type I-inhibitor Dovitinib and the type II-inhibitor Ponatinib reveal the molecular interactions with different types of kinase inhibitors and may assist in the design and development of FGFR4-inhibitors. | ||
| - | + | Structural analysis of the human Fibroblast Growth Factor Receptor 4 Kinase.,Lesca E, Lammens A, Huber R, Augustin M J Mol Biol. 2014 Sep 11. pii: S0022-2836(14)00474-4. doi:, 10.1016/j.jmb.2014.09.004. PMID:25219510<ref>PMID:25219510</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Receptor protein-tyrosine kinase]] | ||
| + | [[Category: Augustin, M.]] | ||
| + | [[Category: Huber, R.]] | ||
| + | [[Category: Lammens, A.]] | ||
| + | [[Category: Lesca, E.]] | ||
| + | [[Category: Dovitinib]] | ||
| + | [[Category: Fibroblast growth factor receptor]] | ||
| + | [[Category: Kinase]] | ||
| + | [[Category: Ponatinb]] | ||
| + | [[Category: Proteros biostructures gmbh]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 10:23, 24 September 2014
Structural analysis of the human Fibroblast Growth Factor Receptor 4
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