1ilq: Difference between revisions

Revision as of 13:28, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ilq.png

Template:STRUCTURE 1ilq

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

Template:ABSTRACT PUBMED 10368283

About this StructureAbout this Structure

1ILQ is a Protein complex structure of sequences from Homo sapiens. Full experimental 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 Tue Jul 1 13:28:17 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1ilq.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1ilq|  PDB=1ilq  |  SCENE=  }}
-'''CXCR-1 N-TERMINAL PEPTIDE BOUND TO INTERLEUKIN-8 (MINIMIZED MEAN)'''
+===CXCR-1 N-TERMINAL PEPTIDE BOUND TO INTERLEUKIN-8 (MINIMIZED MEAN)===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10368283}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10368283 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10368283}}
 ==About this Structure==
-ILQ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ILQ OCA].
+ILQ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ILQ OCA].
 ==Reference==
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 [[Category: Skelton, N J.]]
 [[Category: Cytokine]]
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