1a15: Difference between revisions
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[[Image:1a15.gif|left|200px]]<br /> | [[Image:1a15.gif|left|200px]]<br /><applet load="1a15" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1a15" size=" | |||
caption="1a15, resolution 2.2Å" /> | caption="1a15, resolution 2.2Å" /> | ||
'''SDF-1ALPHA'''<br /> | '''SDF-1ALPHA'''<br /> | ||
==Overview== | ==Overview== | ||
Stromal cell-derived factor-1alpha (SDF-1alpha ) is a member of the | 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. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1A15 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1A15 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9618518 9618518] | 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9618518 9618518] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dealwis, C | [[Category: Dealwis, C G.]] | ||
[[Category: Fernandez, E | [[Category: Fernandez, E J.]] | ||
[[Category: Lolis, E.]] | [[Category: Lolis, E.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: human stromal cell-derived factor-1alpha]] | [[Category: human stromal cell-derived factor-1alpha]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:41 2008'' | ||
Revision as of 12:39, 21 February 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] with as ligand. 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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