1alu
From Proteopedia
Line 1: | Line 1: | ||
- | [[Image:1alu.gif|left|200px]] | + | [[Image:1alu.gif|left|200px]] |
- | + | ||
- | '''HUMAN INTERLEUKIN-6''' | + | {{Structure |
+ | |PDB= 1alu |SIZE=350|CAPTION= <scene name='initialview01'>1alu</scene>, resolution 1.9Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=TLA:L(+)-TARTARIC ACID'>TLA</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''HUMAN INTERLEUKIN-6''' | ||
+ | |||
==Overview== | ==Overview== | ||
Line 10: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
- | 1ALU is a [ | + | 1ALU 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=1ALU OCA]. |
==Reference== | ==Reference== | ||
- | 1.9 A crystal structure of interleukin 6: implications for a novel mode of receptor dimerization and signaling., Somers W, Stahl M, Seehra JS, EMBO J. 1997 Mar 3;16(5):989-97. PMID:[http:// | + | 1.9 A crystal structure of interleukin 6: implications for a novel mode of receptor dimerization and signaling., Somers W, Stahl M, Seehra JS, EMBO J. 1997 Mar 3;16(5):989-97. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9118960 9118960] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
Line 27: | Line 36: | ||
[[Category: signaling]] | [[Category: signaling]] | ||
- | ''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 09:59:18 2008'' |
Revision as of 07:59, 20 March 2008
| |||||||
, resolution 1.9Å | |||||||
---|---|---|---|---|---|---|---|
Ligands: | and | ||||||
Coordinates: | save as pdb, mmCIF, xml |
HUMAN INTERLEUKIN-6
Contents |
Overview
Interleukin 6 (IL-6) has many biological activities in vivo, and deregulation has been implicated in many disease processes. IL-6, a 185 amino acid polypeptide was refolded, purified and crystallized. The crystals diffracted to beyond 1.9 A and the structure was solved using single isomorphous replacement. The X-ray structure of IL-6 is composed of a four helix bundle linked by loops and an additional mini-helix. 157 out of 185 residues are well defined in the final structure, with 18 N-terminal and 8 A-B loop amino acids displaying no interpretable electron density. The three-dimensional structure has been used to construct a model of IL-6 interacting with the IL-6 receptor (alpha-chain) and gp130 (beta-chain) that gives new insight into the process of molecular recognition and signaling. Based on this model, we predict a fourth binding site on IL-6, a low affinity IL-6-IL-6 interaction, which may be necessary for the sequential assembly of a functional hexameric IL-6 receptor complex.
Disease
Known diseases associated with this structure: Kaposi sarcoma, susceptibility to OMIM:[147620], Osteopenia/osteoporosis OMIM:[147620]
About this Structure
1ALU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
1.9 A crystal structure of interleukin 6: implications for a novel mode of receptor dimerization and signaling., Somers W, Stahl M, Seehra JS, EMBO J. 1997 Mar 3;16(5):989-97. PMID:9118960
Page seeded by OCA on Thu Mar 20 09:59:18 2008
Categories: Homo sapiens | Single protein | Seehra, J S. | Somers, W S. | Stahl, M. | SO4 | TLA | Cytokine | Glycoprotein | Interleukin | Receptor | Signaling