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1a15
From Proteopedia
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[[Image:1a15.gif|left|200px]] | [[Image:1a15.gif|left|200px]] | ||
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'''SDF-1ALPHA''' | '''SDF-1ALPHA''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1A15 is a [[Single protein]] structure | + | 1A15 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A15 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Fernandez, E J.]] | [[Category: Fernandez, E J.]] | ||
[[Category: Lolis, E.]] | [[Category: Lolis, E.]] | ||
| - | [[Category: | + | [[Category: Chemokine]] |
| - | [[Category: | + | [[Category: Human stromal cell-derived factor-1alpha]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:39:13 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:39, 2 May 2008
SDF-1ALPHA
Overview
Stromal cell-derived factor-1alpha (SDF-1alpha ) is a member of the chemokine superfamily and functions as a growth factor and chemoattractant through activation of CXCR4/LESTR/Fusin, a G protein-coupled receptor. This receptor also functions as a coreceptor for T-tropic syncytium-inducing strains of HIV-1. SDF-1alpha antagonizes infectivity of these strains by competing with gp120 for binding to the receptor. The crystal structure of a variant SDF-1alpha ([N33A]SDF-1alpha ) prepared by total chemical synthesis has been refined to 2.2-A resolution. Although SDF-1alpha adopts a typical chemokine beta-beta-beta-alpha topology, the packing of the alpha-helix against the beta-sheet is strikingly different. Comparison of SDF-1alpha with other chemokine structures confirms the hypothesis that SDF-1alpha may be either an ancestral protein from which all other chemokines evolved or the chemokine that is the least divergent from a primordial chemokine. The structure of SDF-1alpha reveals a positively charged surface ideal for binding to the negatively charged extracellular loops of the CXCR4 HIV-1 coreceptor. This ionic complementarity is likely to promote the interaction of the mobile N-terminal segment of SDF-1alpha with interhelical sites of the receptor, resulting in a biological response.
About this Structure
1A15 is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Crystal structure of chemically synthesized [N33A] stromal cell-derived factor 1alpha, a potent ligand for the HIV-1 "fusin" coreceptor., Dealwis C, Fernandez EJ, Thompson DA, Simon RJ, Siani MA, Lolis E, Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6941-6. PMID:9618518 Page seeded by OCA on Fri May 2 09:39:13 2008
