1alu
From Proteopedia
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|PDB= 1alu |SIZE=350|CAPTION= <scene name='initialview01'>1alu</scene>, resolution 1.9Å | |PDB= 1alu |SIZE=350|CAPTION= <scene name='initialview01'>1alu</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1alu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alu OCA], [http://www.ebi.ac.uk/pdbsum/1alu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1alu RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147620 147620]], Osteopenia/osteoporosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147620 147620]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Somers, W S.]] | [[Category: Somers, W S.]] | ||
[[Category: Stahl, M.]] | [[Category: Stahl, M.]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: TLA]] | ||
[[Category: cytokine]] | [[Category: cytokine]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
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[[Category: signaling]] | [[Category: signaling]] | ||
| - | ''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 18:42:59 2008'' |
Revision as of 15:43, 30 March 2008
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| , resolution 1.9Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN INTERLEUKIN-6
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.
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 Sun Mar 30 18:42:59 2008
