2i1b: Difference between revisions
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'''CRYSTALLOGRAPHIC REFINEMENT OF INTERLEUKIN-1 BETA AT 2.0 ANGSTROMS RESOLUTION''' | {{Structure | ||
|PDB= 2i1b |SIZE=350|CAPTION= <scene name='initialview01'>2i1b</scene>, resolution 2.0Å | |||
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'''CRYSTALLOGRAPHIC REFINEMENT OF INTERLEUKIN-1 BETA AT 2.0 ANGSTROMS RESOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2I1B is a [ | 2I1B 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=2I1B OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/2602367 2602367] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cytokine]] | [[Category: cytokine]] | ||
''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 17:24:13 2008'' | ||
Revision as of 18:24, 20 March 2008
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CRYSTALLOGRAPHIC REFINEMENT OF INTERLEUKIN-1 BETA AT 2.0 ANGSTROMS RESOLUTION
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Gastric cancer risk after H. pylori infection OMIM:[147720]
About this StructureAbout this Structure
2I1B is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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