2oiq: Difference between revisions

Revision as of 11:28, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2oiq.png

Template:STRUCTURE 2oiq

Crystal Structure of chicken c-Src kinase domain in complex with the cancer drug imatinib.Crystal Structure of chicken c-Src kinase domain in complex with the cancer drug imatinib.

Template:ABSTRACT PUBMED 17355866

About this StructureAbout this Structure

2OIQ is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

c-Src binds to the cancer drug imatinib with an inactive Abl/c-Kit conformation and a distributed thermodynamic penalty., Seeliger MA, Nagar B, Frank F, Cao X, Henderson MN, Kuriyan J, Structure. 2007 Mar;15(3):299-311. PMID:17355866

Page seeded by OCA on Mon Jul 28 11:28:55 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2oiq.gif|left|200px]]
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-'''Crystal Structure of chicken c-Src kinase domain in complex with the cancer drug imatinib.'''
+===Crystal Structure of chicken c-Src kinase domain in complex with the cancer drug imatinib.===
-==Overview==
+<!--
-The cancer drug imatinib inhibits the tyrosine kinases c-Abl, c-Kit, and the PDGF receptor. Imatinib is less effective against c-Src, which is difficult to understand because residues interacting with imatinib in crystal structures of Abl and c-Kit are conserved in c-Src. The crystal structure of the c-Src kinase domain in complex with imatinib closely resembles that of Abl*imatinib and c-Kit*imatinib, and differs significantly from the inactive "Src/CDK" conformation of the Src family kinases. Attempts to increase the affinity of c-Src for imatinib by swapping residues with the corresponding residues in Abl have not been successful, suggesting that the thermodynamic penalty for adoption of the imatinib-binding conformation by c-Src is distributed over a broad region of the structure. Two mutations that are expected to destabilize the inactive Src/CDK conformation increase drug sensitivity 15-fold, suggesting that the free-energy balance between different inactive states is a key to imatinib binding.
+The line below this paragraph, {{ABSTRACT_PUBMED_17355866}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17355866 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17355866}}
 ==About this Structure==
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 [[Category: Seeliger, M A.]]
 [[Category: Src,kinase,imatinib,inactive]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:28:55 2008''