2py3: Difference between revisions

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[[Image:2py3.png|left|200px]]

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~~'''~~Crystal Strucure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic E565G Mutation Responsible for Pfeiffer Syndrome~~'''~~

===Crystal Strucure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic E565G Mutation Responsible for Pfeiffer Syndrome===

~~==Overview==~~

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~~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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_17803937}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17803937 is the PubMed ID number.

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==About this Structure==

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[[Category: Kinase domain fold consisting of n- and c-lobe]]

[[Category: Transferase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 14~~:00:09 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:10:02 2008''

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-[[Image:2py3.jpg|left|200px]]
+{{Seed}}
+[[Image:2py3.png|left|200px]]
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 {{STRUCTURE_2py3|  PDB=2py3  |  SCENE=  }}
-'''Crystal Strucure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic E565G Mutation Responsible for Pfeiffer Syndrome'''
+===Crystal Strucure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic E565G Mutation Responsible for Pfeiffer Syndrome===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17803937}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17803937 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17803937}}
 ==About this Structure==
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 [[Category: Kinase domain fold consisting of n- and c-lobe]]
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 14:00:09 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:10:02 2008''