1alu

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(New page: 200px<br /> <applet load="1alu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1alu, resolution 1.9&Aring;" /> '''HUMAN INTERLEUKIN-6'...)
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caption="1alu, resolution 1.9&Aring;" />
'''HUMAN INTERLEUKIN-6'''<br />
'''HUMAN INTERLEUKIN-6'''<br />
==Overview==
==Overview==
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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.
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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==
==Disease==
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==About this Structure==
==About this Structure==
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1ALU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 and TLA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ALU OCA].
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1ALU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=TLA:'>TLA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALU OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Seehra, J.S.]]
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[[Category: Seehra, J S.]]
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[[Category: Somers, W.S.]]
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[[Category: Somers, W S.]]
[[Category: Stahl, M.]]
[[Category: Stahl, M.]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: signaling]]
[[Category: signaling]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 15:59:38 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:45:56 2008''

Revision as of 09:45, 21 February 2008

Image:1alu.gif

1alu, resolution 1.9Å

Drag the structure with the mouse to rotate

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 with and as ligands. 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

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