1m14: Difference between revisions

Revision as of 22:59, 2 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:1m14.png

Template:STRUCTURE 1m14

Tyrosine Kinase Domain from Epidermal Growth Factor ReceptorTyrosine Kinase Domain from Epidermal Growth Factor Receptor

Template:ABSTRACT PUBMED 12196540

About this StructureAbout this Structure

1M14 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor., Stamos J, Sliwkowski MX, Eigenbrot C, J Biol Chem. 2002 Nov 29;277(48):46265-72. Epub 2002 Aug 23. PMID:12196540

Page seeded by OCA on Wed Jul 2 22:59:19 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1m14.gif|left|200px]]
+{{Seed}}
+[[Image:1m14.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1m14|  PDB=1m14  |  SCENE=  }}
-'''Tyrosine Kinase Domain from Epidermal Growth Factor Receptor'''
+===Tyrosine Kinase Domain from Epidermal Growth Factor Receptor===
-==Overview==
+<!--
-The crystal structure of the kinase domain from the epidermal growth factor receptor (EGFRK) including forty amino acids from the carboxyl-terminal tail has been determined to 2.6-A resolution, both with and without an EGFRK-specific inhibitor currently in Phase III clinical trials as an anti-cancer agent, erlotinib (OSI-774, CP-358,774, Tarceva(TM)). The EGFR family members are distinguished from all other known receptor tyrosine kinases in possessing constitutive kinase activity without a phosphorylation event within their kinase domains. Despite its lack of phosphorylation, we find that the EGFRK activation loop adopts a conformation similar to that of the phosphorylated active form of the kinase domain from the insulin receptor. Surprisingly, key residues of a putative dimerization motif lying between the EGFRK domain and carboxyl-terminal substrate docking sites are found in close contact with the kinase domain. Significant intermolecular contacts involving the carboxyl-terminal tail are discussed with respect to receptor oligomerization.
+The line below this paragraph, {{ABSTRACT_PUBMED_12196540}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12196540 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12196540}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Transferase]]
 [[Category: Tyrosine kinase domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:30:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 22:59:19 2008''