2i1b
From Proteopedia
(New page: 200px<br /> <applet load="2i1b" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i1b, resolution 2.0Å" /> '''CRYSTALLOGRAPHIC REF...) |
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caption="2i1b, resolution 2.0Å" /> | caption="2i1b, resolution 2.0Å" /> | ||
'''CRYSTALLOGRAPHIC REFINEMENT OF INTERLEUKIN-1 BETA AT 2.0 ANGSTROMS RESOLUTION'''<br /> | '''CRYSTALLOGRAPHIC REFINEMENT OF INTERLEUKIN-1 BETA AT 2.0 ANGSTROMS RESOLUTION'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2I1B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2I1B is a [http://en.wikipedia.org/wiki/Single_protein 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=2I1B OCA]. |
==Reference== | ==Reference== | ||
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[[Category: cytokine]] | [[Category: cytokine]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:34:33 2008'' |
Revision as of 15:34, 15 February 2008
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CRYSTALLOGRAPHIC REFINEMENT OF INTERLEUKIN-1 BETA AT 2.0 ANGSTROMS RESOLUTION
Contents |
Overview
The structure of human recombinant interleukin 1 beta (IL-1 beta) has been, refined by a restrained least-squares method to a crystallographic R, factor of 17.2% to 2.0 A resolution. One-hundred sixty-eight solvent, molecules have been located, and isotropic temperature factors for each, atom have been refined. The overall structure is composed of 12, beta-strands that can best be described as forming the four triangular, faces of a tetrahedron with hydrogen bonding resembling normal, antiparallel beta-sheets only at the vertices. The interior of this, tetrahedron is filled by hydrophobic side chains. Analysis of sequence, alignments with IL-1 beta from other mammalian species shows the interior, to be very well conserved with the exterior residues markedly less so., There does not appear to be a clustering of invariant amino acid side, chains on the surface of the molecule, suggesting an area of interaction, with the IL-1 receptor. Comparison of the IL-1 beta structure with IL-1, alpha sequences indicates that IL-1 alpha probably has a similar overall, folding as IL-1 beta but binds to the receptor in a different fashion. The, three-dimensional structure of the IL-1 beta is analyzed in light of what, has been suggested by previously published work on mutants and fragments, of the molecule.
Disease
Known disease associated with this structure: Gastric cancer risk after H. pylori infection OMIM:[147720]
About this Structure
2I1B is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystallographic refinement of interleukin 1 beta at 2.0 A resolution., Priestle JP, Schar HP, Grutter MG, Proc Natl Acad Sci U S A. 1989 Dec;86(24):9667-71. PMID:2602367
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