2i1b

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[[Image:2i1b.jpg|left|200px]]
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{{Structure
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{{STRUCTURE_2i1b| PDB=2i1b | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i1b OCA], [http://www.ebi.ac.uk/pdbsum/2i1b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i1b RCSB]</span>
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'''CRYSTALLOGRAPHIC REFINEMENT OF INTERLEUKIN-1 BETA AT 2.0 ANGSTROMS RESOLUTION'''
'''CRYSTALLOGRAPHIC REFINEMENT OF INTERLEUKIN-1 BETA AT 2.0 ANGSTROMS RESOLUTION'''
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[[Category: Priestle, J P.]]
[[Category: Priestle, J P.]]
[[Category: Schaer, H P.]]
[[Category: Schaer, H P.]]
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[[Category: cytokine]]
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[[Category: Cytokine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:57:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:38:25 2008''
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Revision as of 03:57, 4 May 2008

Image:2i1b.jpg

Template:STRUCTURE 2i1b

CRYSTALLOGRAPHIC REFINEMENT OF INTERLEUKIN-1 BETA AT 2.0 ANGSTROMS RESOLUTION


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.

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 Page seeded by OCA on Sun May 4 06:57:34 2008

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