3il8
From Proteopedia
CRYSTAL STRUCTURE OF INTERLEUKIN 8: SYMBIOSIS OF NMR AND CRYSTALLOGRAPHY
Structural highlights
Function[IL8_HUMAN] IL-8 is a chemotactic factor that attracts neutrophils, basophils, and T-cells, but not monocytes. It is also involved in neutrophil activation. It is released from several cell types in response to an inflammatory stimulus. IL-8(6-77) has a 5-10-fold higher activity on neutrophil activation, IL-8(5-77) has increased activity on neutrophil activation and IL-8(7-77) has a higher affinity to receptors CXCR1 and CXCR2 as compared to IL-8(1-77), respectively.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of a host defense system chemotactic factor, interleukin 8, has been solved by molecular replacement using as a model the solution structure derived from nuclear magnetic resonance experiments. The structure was refined with 2 A x-ray data to an R factor of 0.187 (0.217 at 1.6 A). A comparison indicates some potential differences between the structure in solution and in the crystalline state. Our analysis also predicts that residues 4 through 9 on the amino terminus and the beta-bend, which includes His-33, may be important for receptor binding. Crystal structure of interleukin 8: symbiosis of NMR and crystallography.,Baldwin ET, Weber IT, St Charles R, Xuan JC, Appella E, Yamada M, Matsushima K, Edwards BF, Clore GM, Gronenborn AM, et al. Proc Natl Acad Sci U S A. 1991 Jan 15;88(2):502-6. PMID:1988949[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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