1hzi
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1hzi |SIZE=350|CAPTION= <scene name='initialview01'>1hzi</scene>, resolution 2.05Å | |PDB= 1hzi |SIZE=350|CAPTION= <scene name='initialview01'>1hzi</scene>, resolution 2.05Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1rcb|1rcb]], [[2int|2int]], [[1hik|1hik]], [[1hij|1hij]], [[1iar|1iar]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hzi OCA], [http://www.ebi.ac.uk/pdbsum/1hzi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hzi RCSB]</span> | ||
}} | }} | ||
| Line 14: | Line 17: | ||
==Overview== | ==Overview== | ||
Interleukin 4 (IL-4) is a pleiotropic cytokine which induces T-cell differentiation and class switching of B cells. It therefore plays a central role in the development of allergies and asthma. An IL-4 variant in which Glu9 was mutated to alanine shows an 800-fold drop in binding affinity towards its high-affinity receptor chain. As shown by surface plasmon resonance measurements, this mostly arises from a decreased association rate. Here, the crystal structure of this mutant is reported. It reveals that the protein has a virtually identical structure to the wild type, showing that the unusual behaviour of the mutated protein is not a consequence of misfolding. The possibility that polar interactions in the encounter complex have a steering effect is discussed. | Interleukin 4 (IL-4) is a pleiotropic cytokine which induces T-cell differentiation and class switching of B cells. It therefore plays a central role in the development of allergies and asthma. An IL-4 variant in which Glu9 was mutated to alanine shows an 800-fold drop in binding affinity towards its high-affinity receptor chain. As shown by surface plasmon resonance measurements, this mostly arises from a decreased association rate. Here, the crystal structure of this mutant is reported. It reveals that the protein has a virtually identical structure to the wild type, showing that the unusual behaviour of the mutated protein is not a consequence of misfolding. The possibility that polar interactions in the encounter complex have a steering effect is discussed. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: AIDS, slow progression to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147781 147781]], Atopy, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147781 147781]] | ||
==About this Structure== | ==About this Structure== | ||
| Line 28: | Line 28: | ||
[[Category: Hulsmeyer, M.]] | [[Category: Hulsmeyer, M.]] | ||
[[Category: Scheufler, C.]] | [[Category: Scheufler, C.]] | ||
| - | [[Category: SO4]] | ||
[[Category: 4-helix-bundle]] | [[Category: 4-helix-bundle]] | ||
[[Category: cytokine]] | [[Category: cytokine]] | ||
[[Category: il-4]] | [[Category: il-4]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:12:27 2008'' |
Revision as of 18:12, 30 March 2008
| |||||||
| , resolution 2.05Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 1rcb, 2int, 1hik, 1hij, 1iar
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
INTERLEUKIN-4 MUTANT E9A
Overview
Interleukin 4 (IL-4) is a pleiotropic cytokine which induces T-cell differentiation and class switching of B cells. It therefore plays a central role in the development of allergies and asthma. An IL-4 variant in which Glu9 was mutated to alanine shows an 800-fold drop in binding affinity towards its high-affinity receptor chain. As shown by surface plasmon resonance measurements, this mostly arises from a decreased association rate. Here, the crystal structure of this mutant is reported. It reveals that the protein has a virtually identical structure to the wild type, showing that the unusual behaviour of the mutated protein is not a consequence of misfolding. The possibility that polar interactions in the encounter complex have a steering effect is discussed.
About this Structure
1HZI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of interleukin 4 mutant E9A suggests polar steering in receptor-complex formation., Hulsmeyer M, Scheufler C, Dreyer MK, Acta Crystallogr D Biol Crystallogr. 2001 Sep;57(Pt 9):1334-6. Epub 2001, Aug 23. PMID:11526337
Page seeded by OCA on Sun Mar 30 21:12:27 2008
