2py3: Difference between revisions
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|PDB= 2py3 |SIZE=350|CAPTION= <scene name='initialview01'>2py3</scene>, resolution 2.3Å | |PDB= 2py3 |SIZE=350|CAPTION= <scene name='initialview01'>2py3</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ABG:ADENOSINE+5'-[BETA,GAMMA-METHYLENE]TRIPHOSPHATE'>ABG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <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> | ||
|GENE= FGFR2, BEK, KSAM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= FGFR2, BEK, KSAM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2psq|2PSQ]], [[2pvf|2PVF]], [[2pvy|2PVY]], [[2pwl|2PWL]], [[2pz5|2PZ5]], [[2pzp|2PZP]], [[2pzr|2PZR]], [[2q0b|2Q0B]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2py3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2py3 OCA], [http://www.ebi.ac.uk/pdbsum/2py3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2py3 RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
Activating mutations in the tyrosine kinase domain of receptor tyrosine kinases (RTKs) cause cancer and skeletal disorders. Comparison of the crystal structures of unphosphorylated and phosphorylated wild-type FGFR2 kinase domains with those of seven unphosphorylated pathogenic mutants reveals an autoinhibitory "molecular brake" mediated by a triad of residues in the kinase hinge region of all FGFRs. Structural analysis shows that many other RTKs, including PDGFRs, VEGFRs, KIT, CSF1R, FLT3, TEK, and TIE, are also subject to regulation by this brake. Pathogenic mutations activate FGFRs and other RTKs by disengaging the brake either directly or indirectly. | Activating mutations in the tyrosine kinase domain of receptor tyrosine kinases (RTKs) cause cancer and skeletal disorders. Comparison of the crystal structures of unphosphorylated and phosphorylated wild-type FGFR2 kinase domains with those of seven unphosphorylated pathogenic mutants reveals an autoinhibitory "molecular brake" mediated by a triad of residues in the kinase hinge region of all FGFRs. Structural analysis shows that many other RTKs, including PDGFRs, VEGFRs, KIT, CSF1R, FLT3, TEK, and TIE, are also subject to regulation by this brake. Pathogenic mutations activate FGFRs and other RTKs by disengaging the brake either directly or indirectly. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Chen, H.]] | [[Category: Chen, H.]] | ||
[[Category: Mohammadi, M.]] | [[Category: Mohammadi, M.]] | ||
[[Category: kinase domain fold consisting of n- and c-lobe]] | [[Category: kinase domain fold consisting of n- and c-lobe]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:42:15 2008'' | ||
