5wdz
From Proteopedia
(Difference between revisions)
m (Protected "5wdz" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Structure of monomeric Interleukin-8 (1-66)== | |
| + | <StructureSection load='5wdz' size='340' side='right' caption='[[5wdz]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5wdz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WDZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WDZ FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wdz OCA], [http://pdbe.org/5wdz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wdz RCSB], [http://www.ebi.ac.uk/pdbsum/5wdz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wdz ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/IL8_HUMAN 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.<ref>PMID:2145175</ref> <ref>PMID:2212672</ref> <ref>PMID:11978786</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The structure of monomeric human chemokine IL-8 (residues 1-66) was determined in aqueous solution by NMR spectroscopy. The structure of the monomer is similar to that of each subunit in the dimeric full-length protein (residues 1-72), with the main differences being the location of the N-loop (residues 10-22) relative to the C-terminal alpha-helix and the position of the side chain of phenylalanine 65 near the truncated dimerization interface (residues 67-72). NMR was used to analyze the interactions of monomeric IL-8 (1-66) with ND-CXCR1 (residues 1-38), a soluble polypeptide corresponding to the N-terminal portion of the ligand binding site (Binding Site-I) of the chemokine receptor CXCR1 in aqueous solution, and with 1TM-CXCR1 (residues 1-72), a membrane-associated polypeptide that includes the same N-terminal portion of the binding site, the first trans-membrane helix, and the first intracellular loop of the receptor in nanodiscs. The presence of neither the first transmembrane helix of the receptor nor the lipid bilayer significantly affected the interactions of IL-8 with Binding Site-I of CXCR1. | ||
| - | + | Structure of monomeric Interleukin-8 and its interactions with the N-terminal Binding Site-I of CXCR1 by solution NMR spectroscopy.,Berkamp S, Park SH, De Angelis AA, Marassi FM, Opella SJ J Biomol NMR. 2017 Nov 15. pii: 10.1007/s10858-017-0128-3. doi:, 10.1007/s10858-017-0128-3. PMID:29143165<ref>PMID:29143165</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5wdz" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Berkamp, S]] | [[Category: Berkamp, S]] | ||
| + | [[Category: Marassi, F M]] | ||
| + | [[Category: Opella, S J]] | ||
| + | [[Category: Chemokine-fold]] | ||
| + | [[Category: Cytokine]] | ||
| + | [[Category: Interleukin-8]] | ||
Revision as of 06:12, 29 November 2017
Structure of monomeric Interleukin-8 (1-66)
| |||||||||||
