1a15: Difference between revisions
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[[Image:1a15.gif|left|200px]] | [[Image:1a15.gif|left|200px]] | ||
'''SDF-1ALPHA''' | {{Structure | ||
|PDB= 1a15 |SIZE=350|CAPTION= <scene name='initialview01'>1a15</scene>, resolution 2.2Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''SDF-1ALPHA''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1A15 is a [ | 1A15 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A15 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9618518 9618518] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dealwis, C G.]] | [[Category: Dealwis, C G.]] | ||
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[[Category: human stromal cell-derived factor-1alpha]] | [[Category: human stromal cell-derived factor-1alpha]] | ||
''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 09:51:24 2008'' | ||
Revision as of 10:51, 20 March 2008
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SDF-1ALPHA
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: AIDS, resistance to OMIM:[600835]
About this StructureAbout this Structure
1A15 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
ReferenceReference
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
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