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|3il8, resolution 2.00Å ()|
CRYSTAL STRUCTURE OF INTERLEUKIN 8: SYMBIOSIS OF NMR AND CRYSTALLOGRAPHY
The 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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Baldwin ET, Weber IT, St Charles R, Xuan JC, Appella E, Yamada M, Matsushima K, Edwards BF, Clore GM, Gronenborn AM, et al.. Crystal structure of interleukin 8: symbiosis of NMR and crystallography. Proc Natl Acad Sci U S A. 1991 Jan 15;88(2):502-6. PMID:1988949
- Richardson JS, Richardson DC. Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2754-9. PMID:11880627 doi:10.1073/pnas.052706099
- Liang S, Li L, Hsu WL, Pilcher MN, Uversky V, Zhou Y, Dunker AK, Meroueh SO. Exploring the molecular design of protein interaction sites with molecular dynamics simulations and free energy calculations. Biochemistry. 2009 Jan 20;48(2):399-414. PMID:19113835 doi:10.1021/bi8017043