1rod

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CHIMERIC PROTEIN OF INTERLEUKIN 8 AND HUMAN MELANOMA GROWTH STIMULATING ACTIVITY PROTEIN, NMR

Structural highlights

1rod is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 8 models
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

A 72-amino-acid chimeric protein, Chi1, was constructed from the N-terminal part of interleukin 8, IL-8-(1-53), and the C-terminal part of melanoma growth stimulatory activity, MGSA-(54-72). Chi1 protein showed receptor-binding specificity and biological activity similar, but not identical to IL-8 and decidedly different from MGSA. The structure of Chi1 was determined in solution by two-dimensional NMR and molecular-dynamics calculations. The structure resembled the structures of MGSA and IL-8 closely, containing a triple-stranded beta-sheet in the IL-8 part and an amphipathic alpha-helix in the MGSA part. Chi1 formed dimers at millimolar concentrations via the first strand from the N-terminus, analogous to IL-8 and MGSA. In contrast to the latter molecules, however, the alpha-helix of Chi1 did not pack against the beta-sheet part, but was an independent structural element. This structural difference could be explained mainly by the modulation of hydrophobic interactions between the helix and the rest of the protein in Chi1 as compared to IL-8 and MGSA. It is concluded that tight helix packing is not required for receptor binding and biological activity of Chi1.

Structure and activity of a chimeric interleukin-8-melanoma-growth-stimulatory-activity protein.,Sticht H, Auer M, Schmitt B, Besemer J, Horcher M, Kirsch T, Lindley IJ, Rosch P Eur J Biochem. 1996 Jan 15;235(1-2):26-35. PMID:8631339[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
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NMR mapping of RANTES surfaces interacting with CCR5 using linked extracellular domains.
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See Also

References

  1. ↑ Van Damme J, Rampart M, Conings R, Decock B, Van Osselaer N, Willems J, Billiau A. The neutrophil-activating proteins interleukin 8 and beta-thromboglobulin: in vitro and in vivo comparison of NH2-terminally processed forms. Eur J Immunol. 1990 Sep;20(9):2113-8. PMID:2145175 doi:http://dx.doi.org/10.1002/eji.1830200933
  2. ↑ Hebert CA, Luscinskas FW, Kiely JM, Luis EA, Darbonne WC, Bennett GL, Liu CC, Obin MS, Gimbrone MA Jr, Baker JB. Endothelial and leukocyte forms of IL-8. Conversion by thrombin and interactions with neutrophils. J Immunol. 1990 Nov 1;145(9):3033-40. PMID:2212672
  3. ↑ Schutyser E, Struyf S, Proost P, Opdenakker G, Laureys G, Verhasselt B, Peperstraete L, Van de Putte I, Saccani A, Allavena P, Mantovani A, Van Damme J. Identification of biologically active chemokine isoforms from ascitic fluid and elevated levels of CCL18/pulmonary and activation-regulated chemokine in ovarian carcinoma. J Biol Chem. 2002 Jul 5;277(27):24584-93. Epub 2002 Apr 26. PMID:11978786 doi:http://dx.doi.org/10.1074/jbc.M112275200
  4. ↑ Sticht H, Auer M, Schmitt B, Besemer J, Horcher M, Kirsch T, Lindley IJ, Rosch P. Structure and activity of a chimeric interleukin-8-melanoma-growth-stimulatory-activity protein. Eur J Biochem. 1996 Jan 15;235(1-2):26-35. PMID:8631339

Contents


PDB ID 1rod

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