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1h59
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(New page: 200px<br /> <applet load="1h59" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h59, resolution 2.1Å" /> '''COMPLEX OF IGFBP-5 W...)
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Revision as of 15:06, 12 November 2007
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COMPLEX OF IGFBP-5 WITH IGF-I
Contents |
Overview
Insulin-like growth factors (IGFs) are key regulators of cell, proliferation, differentiation and transformation, and are thus pivotal in, cancer, especially breast, prostate and colon neoplasms. They are also, important in many neurological and bone disorders. Their potent mitogenic, and anti-apoptotic actions depend primarily on their availability to bind, to the cell surface IGF-I receptor. In circulation and interstitial, fluids, IGFs are largely unavailable as they are tightly associated with, IGF-binding proteins (IGFBPs) and are released after IGFBP proteolysis., Here we report the 2.1 A crystal structure of the complex of IGF-I bound, to the N-terminal IGF-binding domain of IGFBP-5 (mini-IGFBP-5), a, prototype interaction for all N-terminal domains of the IGFBP family. The, principal interactions in the complex comprise interlaced hydrophobic side, chains that protrude from both IGF-I and the IGFBP-5 fragment and a, surrounding network of polar interactions. A solvent-exposed hydrophobic, patch is located on the IGF-I pole opposite to the mini-IGFBP-5 binding, region and marks the IGF-I receptor binding site.
Disease
Known disease associated with this structure: Growth retardation with deafness and mental retardation due to IGF1 deficiency OMIM:[147440]
About this Structure
1H59 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The interaction of insulin-like growth factor-I with the N-terminal domain of IGFBP-5., Zeslawski W, Beisel HG, Kamionka M, Kalus W, Engh RA, Huber R, Lang K, Holak TA, EMBO J. 2001 Jul 16;20(14):3638-44. PMID:11447105
Page seeded by OCA on Mon Nov 12 17:13:02 2007
