1qe6
From Proteopedia
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| - | [[Image:1qe6.gif|left|200px]] | + | [[Image:1qe6.gif|left|200px]] |
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| - | '''INTERLEUKIN-8 WITH AN ADDED DISULFIDE BETWEEN RESIDUES 5 AND 33 (L5C/H33C)''' | + | {{Structure |
| + | |PDB= 1qe6 |SIZE=350|CAPTION= <scene name='initialview01'>1qe6</scene>, resolution 2.35Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''INTERLEUKIN-8 WITH AN ADDED DISULFIDE BETWEEN RESIDUES 5 AND 33 (L5C/H33C)''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QE6 is a [ | + | 1QE6 is a [[Single protein]] structure of sequence 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=1QE6 OCA]. |
==Reference== | ==Reference== | ||
| - | Receptor-binding conformation of the "ELR" motif of IL-8: X-ray structure of the L5C/H33C variant at 2.35 A resolution., Gerber N, Lowman H, Artis DR, Eigenbrot C, Proteins. 2000 Mar 1;38(4):361-7. PMID:[http:// | + | Receptor-binding conformation of the "ELR" motif of IL-8: X-ray structure of the L5C/H33C variant at 2.35 A resolution., Gerber N, Lowman H, Artis DR, Eigenbrot C, Proteins. 2000 Mar 1;38(4):361-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10707023 10707023] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: intercrine alpha family]] | [[Category: intercrine alpha family]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:36:22 2008'' |
Revision as of 11:36, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
INTERLEUKIN-8 WITH AN ADDED DISULFIDE BETWEEN RESIDUES 5 AND 33 (L5C/H33C)
Contents |
Overview
The "ELR" (Glu-Leu-Arg) tripeptide sequence near the N-terminus of interleukin-8 (IL-8) contributes a large part of the receptor binding free energy. Prior X-ray and nuclear magnetic resonance (NMR) structures of IL-8 have shown this region of the molecule to be highly mobile. We reasoned that a hydrophobic interaction between the leucine and the neighboring beta-turn might exist in the receptor binding conformation of the N-terminus. To test this hypothesis, we mutated two residues to cysteine and connected the N-terminus to the beta-turn. The mutant retains receptor binding affinity reasonably close to wild type and allows the characterization of a high-affinity conformation that may be useful in the design of small IL-8 mimics. The L5C/H33C mutant is refined to R-values of R = 20.6% and Rfree = 27.7% at 2.35 A resolution. Other receptor binding determinants reside in the "N-loop" found after "ELR" and preceding the first beta-strand. All available structures of IL-8 have been found with one of two distinct N-loop conformations. One of these is relevant for receptor binding, based on NMR results with receptor peptides. The other conformation obscures the receptor-peptide binding surface and may have an undetermined but necessarily different function.
Disease
Known disease associated with this structure: AIDS, slow progression to OMIM:[146929]
About this Structure
1QE6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Receptor-binding conformation of the "ELR" motif of IL-8: X-ray structure of the L5C/H33C variant at 2.35 A resolution., Gerber N, Lowman H, Artis DR, Eigenbrot C, Proteins. 2000 Mar 1;38(4):361-7. PMID:10707023
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