2sdf

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2sdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2sdf OCA], [http://www.ebi.ac.uk/pdbsum/2sdf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2sdf RCSB]</span>
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'''SOLUTION NMR STRUCTURE OF STROMAL CELL-DERIVED FACTOR-1 (SDF-1), 30 STRUCTURES'''
'''SOLUTION NMR STRUCTURE OF STROMAL CELL-DERIVED FACTOR-1 (SDF-1), 30 STRUCTURES'''
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[[Category: Rajarathnam, K.]]
[[Category: Rajarathnam, K.]]
[[Category: Sykes, B D.]]
[[Category: Sykes, B D.]]
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[[Category: chemokine]]
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[[Category: Chemokine]]
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[[Category: cytokine]]
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[[Category: Cytokine]]
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[[Category: g-coupled receptor]]
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[[Category: G-coupled receptor]]
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[[Category: protein synthesis]]
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[[Category: Protein synthesis]]
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[[Category: sdf-1]]
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[[Category: Sdf-1]]
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[[Category: solution structure]]
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[[Category: Solution structure]]
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[[Category: stromal cell-derived factor-1]]
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[[Category: Stromal cell-derived factor-1]]
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Revision as of 14:17, 4 May 2008

Template:STRUCTURE 2sdf

SOLUTION NMR STRUCTURE OF STROMAL CELL-DERIVED FACTOR-1 (SDF-1), 30 STRUCTURES


Overview

The three-dimensional structure of stromal cell-derived factor-1 (SDF-1) was determined by NMR spectroscopy. SDF-1 is a monomer with a disordered N-terminal region (residues 1-8), and differs from other chemokines in the packing of the hydrophobic core and surface charge distribution. Results with analogs showed that the N-terminal eight residues formed an important receptor binding site; however, only Lys-1 and Pro-2 were directly involved in receptor activation. Modification to Lys-1 and/or Pro-2 resulted in loss of activity, but generated potent SDF-1 antagonists. Residues 12-17 of the loop region, which we term the RFFESH motif, unlike the N-terminal region, were well defined in the SDF-1 structure. The RFFESH formed a receptor binding site, which we propose to be an important initial docking site of SDF-1 with its receptor. The ability of the SDF-1 analogs to block HIV-1 entry via CXCR4, which is a HIV-1 coreceptor for the virus in addition to being the receptor for SDF-1, correlated with their affinity for CXCR4. Activation of the receptor is not required for HIV-1 inhibition.

About this Structure

2SDF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Solution structure and basis for functional activity of stromal cell-derived factor-1; dissociation of CXCR4 activation from binding and inhibition of HIV-1., Crump MP, Gong JH, Loetscher P, Rajarathnam K, Amara A, Arenzana-Seisdedos F, Virelizier JL, Baggiolini M, Sykes BD, Clark-Lewis I, EMBO J. 1997 Dec 1;16(23):6996-7007. PMID:9384579 Page seeded by OCA on Sun May 4 17:17:43 2008

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