1ilq: Difference between revisions

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[[Image:1ilq.gif|left|200px]]
[[Image:1ilq.gif|left|200px]]


{{Structure
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|PDB= 1ilq |SIZE=350|CAPTION= <scene name='initialview01'>1ilq</scene>
The line below this paragraph, containing "STRUCTURE_1ilq", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=ACA:6-AMINOHEXANOIC+ACID'>ACA</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>
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|ACTIVITY=  
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|DOMAIN=
{{STRUCTURE_1ilq| PDB=1ilq  | SCENE= }}  
|RELATEDENTRY=[[1ilp|1ILP]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ilq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ilq OCA], [http://www.ebi.ac.uk/pdbsum/1ilq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ilq RCSB]</span>
}}


'''CXCR-1 N-TERMINAL PEPTIDE BOUND TO INTERLEUKIN-8 (MINIMIZED MEAN)'''
'''CXCR-1 N-TERMINAL PEPTIDE BOUND TO INTERLEUKIN-8 (MINIMIZED MEAN)'''
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[[Category: Quan, C.]]
[[Category: Quan, C.]]
[[Category: Skelton, N J.]]
[[Category: Skelton, N J.]]
[[Category: cytokine]]
[[Category: Cytokine]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:08:02 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:21:27 2008''

Revision as of 20:08, 2 May 2008

File:1ilq.gif

Template:STRUCTURE 1ilq

CXCR-1 N-TERMINAL PEPTIDE BOUND TO INTERLEUKIN-8 (MINIMIZED MEAN)


OverviewOverview

BACKGROUND: Interactions between CXC chemokines (e.g. interleukin-8, IL-8) and their receptors (e.g. CXCR-1) have a key role in host defense and disease by attracting and upregulating neutrophils to sites of inflammation. The transmembrane nature of the receptor impedes structure-based understanding of ligand interactions. Linear peptides based on the N-terminal, extracellular portion of the receptor CXCR-1 do bind to IL-8, however, and inhibit the binding of IL-8 to the full-length receptor. RESULTS: The NMR solution structure of the complex formed between IL-8 and one such receptor-based peptide indicates that a cleft between a loop and a beta hairpin constitute part of the receptor interaction surface on IL-8. Nine residues from the C terminus of the receptor peptide (corresponding to Pro21-Pro29 of CXCR-1) occupy the cleft in an extended fashion. Intermolecular contacts are mostly hydrophobic and sidechain mediated. CONCLUSIONS: The results offer the first details at an atomic level of the interaction between a chemokine and its receptor. Consideration of other biochemical data allow extrapolation to a model for the interaction of IL-8 with the full-length receptor. In this model, the heparin-binding residues of IL-8 are exposed, thereby allowing presentation of the chemokine from endothelial cell-surface glycosaminoglycans. This first glimpse of how IL-8 binds to its receptor provides a foundation for the structure-based design of chemokine antagonists.

About this StructureAbout this Structure

1ILQ is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structure of a CXC chemokine-receptor fragment in complex with interleukin-8., Skelton NJ, Quan C, Reilly D, Lowman H, Structure. 1999 Feb 15;7(2):157-68. PMID:10368283 Page seeded by OCA on Fri May 2 20:08:02 2008

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