1VMC
STROMA CELL-DERIVED FACTOR-1ALPHA (SDF-1ALPHA)
Summary for 1VMC
| Entry DOI | 10.2210/pdb1vmc/pdb |
| Descriptor | Stromal cell-derived factor 1 (1 entity in total) |
| Functional Keywords | cxc-chemokine, cytokine |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: P48061 |
| Total number of polymer chains | 1 |
| Total formula weight | 8343.80 |
| Authors | Gozansky, E.K.,Clore, G.M. (deposition date: 2004-09-20, release date: 2005-03-01, Last modification date: 2023-12-27) |
| Primary citation | Gozansky, E.K.,Louis, J.M.,Caffrey, M.,Clore, G.M. Mapping the binding of the N-terminal extracellular tail of the CXCR4 receptor to stromal cell-derived factor-1alpha. J.Mol.Biol., 345:651-658, 2005 Cited by PubMed Abstract: The solution structure of monomeric stromal cell-derived factor-1alpha (SDF-1alpha), the natural ligand for the CXCR4 G-coupled receptor, has been solved by multidimensional heteronuclear NMR spectroscopy. The structure has a characteristic chemokine fold and is in excellent agreement with the individual subunits observed in the crystal structures of dimeric SDF-1alpha. Using various peptides derived from the N-terminal extracellular tail of the CXCR4 receptor, we show that the principal determinants of binding reside in the N-terminal 17 residues of CXCR4, with a major contribution from the first six residues. From 15N/1HN chemical shift pertubation studies we show that the interaction surface on SDF-1alpha is formed by the undersurface of the three-stranded antiparallel beta-sheet bounded by the N-terminal loop on one side and the C-terminal helix on the other. This surface overlaps with but is not identical to that mapped on several other chemokines for the binding of equivalent peptides derived from their respective receptors. PubMed: 15588815DOI: 10.1016/j.jmb.2004.11.003 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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