1jqh: Difference between revisions

Revision as of 20:38, 1 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:1jqh.png

Template:STRUCTURE 1jqh

IGF-1 receptor kinase domainIGF-1 receptor kinase domain

Template:ABSTRACT PUBMED 11591350

About this StructureAbout this Structure

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

ReferenceReference

Crystal structure of bisphosphorylated IGF-1 receptor kinase: insight into domain movements upon kinase activation., Pautsch A, Zoephel A, Ahorn H, Spevak W, Hauptmann R, Nar H, Structure. 2001 Oct;9(10):955-65. PMID:11591350

Page seeded by OCA on Tue Jul 1 20:38:43 2008

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OCA

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-'''IGF-1 receptor kinase domain'''
+===IGF-1 receptor kinase domain===
-==Overview==
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-BACKGROUND: The insulin-like growth-factor-1 (IGF-1) receptor, which is widely expressed in cells that have undergone oncogenic transformation, is emerging as a novel target in cancer therapy. IGF-1-induced receptor activation results in autophosphorylation of cytoplasmic kinase domains and enhances their capability to phosphorylate downstream substrates. Structures of the homologous insulin receptor kinase (IRK) exist in an open, unphosphorylated form and a closed, trisphosphorylated form. RESULTS: We have determined the 2.1 A crystal structure of the IGF-1 receptor protein tyrosine kinase domain phosphorylated at two tyrosine residues within the activation loop (IGF-1RK2P) and bound to an ATP analog. The ligand is not in a conformation compatible with phosphoryl transfer, and the activation loop is partially disordered. Compared to the homologous insulin receptor kinase, IGF-1RK2P is trapped in a half-closed, previously unobserved conformation. Observed domain movements can be dissected into two orthogonal rotational components. CONCLUSIONS: Conformational changes upon kinase activation are triggered by the degree of phosphorylation and are crucially dependent on the conformation of the proximal end of the kinase activation loop. This IGF-1RK structure will provide a molecular basis for the design of selective antioncogenic therapeutic agents.
+The line below this paragraph, {{ABSTRACT_PUBMED_11591350}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Zoephel, A.]]
 [[Category: Protein kinase fold]]
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