2sdf
|
SOLUTION NMR STRUCTURE OF STROMAL CELL-DERIVED FACTOR-1 (SDF-1), 30 STRUCTURES
OverviewOverview
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 StructureAbout this Structure
2SDF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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 Thu Nov 8 14:57:27 2007