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| | {{STRUCTURE_1jqh| PDB=1jqh | SCENE= }} | | {{STRUCTURE_1jqh| PDB=1jqh | SCENE= }} |
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| - | '''IGF-1 receptor kinase domain'''
| + | ===IGF-1 receptor kinase domain=== |
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| - | ==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 |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11591350 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11591350}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Zoephel, A.]] | | [[Category: Zoephel, A.]] |
| | [[Category: Protein kinase fold]] | | [[Category: Protein kinase fold]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:38:59 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:38:43 2008'' |
Revision as of 17:38, 1 July 2008
Template:STRUCTURE 1jqh
IGF-1 receptor kinase domain
Template:ABSTRACT PUBMED 11591350
About this Structure
1JQH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
