1m7n
From Proteopedia
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| - | [[Image:1m7n.gif|left|200px]] | + | [[Image:1m7n.gif|left|200px]] |
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| - | '''Crystal Structure of Unactivated APO Insulin-like Growth Factor-1 Receptor Kinase Domain''' | + | {{Structure |
| + | |PDB= 1m7n |SIZE=350|CAPTION= <scene name='initialview01'>1m7n</scene>, resolution 2.7Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Crystal Structure of Unactivated APO Insulin-like Growth Factor-1 Receptor Kinase Domain''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1M7N is a [ | + | 1M7N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7N OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the Apo, unactivated insulin-like growth factor-1 receptor kinase. Implication for inhibitor specificity., Munshi S, Kornienko M, Hall DL, Reid JC, Waxman L, Stirdivant SM, Darke PL, Kuo LC, J Biol Chem. 2002 Oct 11;277(41):38797-802. Epub 2002 Jul 22. PMID:[http:// | + | Crystal structure of the Apo, unactivated insulin-like growth factor-1 receptor kinase. Implication for inhibitor specificity., Munshi S, Kornienko M, Hall DL, Reid JC, Waxman L, Stirdivant SM, Darke PL, Kuo LC, J Biol Chem. 2002 Oct 11;277(41):38797-802. Epub 2002 Jul 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12138114 12138114] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:39:57 2008'' |
Revision as of 10:40, 20 March 2008
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| , resolution 2.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Unactivated APO Insulin-like Growth Factor-1 Receptor Kinase Domain
Contents |
Overview
The x-ray structure of the unactivated kinase domain of insulin-like growth factor-1 receptor (IGFRK-0P) is reported here at 2.7 A resolution. IGFRK-0P is composed of two lobes connected by a hinge region. The N-terminal lobe of the kinase is a twisted beta-sheet flanked by a single helix, and the C-terminal lobe comprises eight alpha-helices and four short beta-strands. The ATP binding pocket and the catalytic center reside at the interface of the two lobes. Despite the overall similarity to other receptor tyrosine kinases, three notable conformational modifications are observed: 1) this kinase adopts a more closed structure, with its two lobes rotated further toward each other; 2) the conformation of the proximal end of the activation loop (residues 1121-1129) is different; 3) the orientation of the nucleotide-binding loop is altered. Collectively, these alterations lead to a different ATP-binding pocket that might impact on inhibitor designs for IGFRK-0P. Two molecules of IGFRK-0P are seen in the asymmetric unit; they are associated as a dimer with their ATP binding clefts facing each other. The ordered N terminus of one monomer approaches the active site of the other, suggesting that the juxtamembrane region of one molecule could come into close proximity to the active site of the other.
Disease
Known disease associated with this structure: Intrauterine and postnatal growth retardation OMIM:[147370]
About this Structure
1M7N is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Apo, unactivated insulin-like growth factor-1 receptor kinase. Implication for inhibitor specificity., Munshi S, Kornienko M, Hall DL, Reid JC, Waxman L, Stirdivant SM, Darke PL, Kuo LC, J Biol Chem. 2002 Oct 11;277(41):38797-802. Epub 2002 Jul 22. PMID:12138114
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