Literature DB >> 1553379

Functional implications of interleukin-1 beta based on the three-dimensional structure.

B Veerapandian1, G L Gilliland, R Raag, A L Svensson, Y Masui, Y Hirai, T L Poulos.   

Abstract

The molecular structure of interleukin-1 beta, a hormone-like cytokine with roles in several disease processes, has been determined at 2.0 A resolution and refined to a crystallographic R-factor of 0.19. The framework of this molecule consists of 12 antiparallel beta-strands exhibiting pseudo-3-fold symmetry. Six of the strands make up a beta-barrel with polar residues concentrated at either end. Analysis of the three-dimensional structure, together with results from site-directed mutagenesis and biochemical and immunological studies, suggest that the core of the beta-barrel plays an important functional role. A large patch of charged residues on one end of the barrel is proposed as the binding surface with which IL-1 interacts with its receptor.

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Year:  1992        PMID: 1553379     DOI: 10.1002/prot.340120103

Source DB:  PubMed          Journal:  Proteins        ISSN: 0887-3585


  23 in total

1.  Structure and function of interleukin-1, based on crystallographic and modeling studies.

Authors:  B Veerapandian
Journal:  Biophys J       Date:  1992-04       Impact factor: 4.033

2.  Molecular dynamics free energy calculations to assess the possibility of water existence in protein nonpolar cavities.

Authors:  Masataka Oikawa; Yoshiteru Yonetani
Journal:  Biophys J       Date:  2010-06-16       Impact factor: 4.033

3.  β-Bulge triggers route-switching on the functional landscape of interleukin-1β.

Authors:  Dominique T Capraro; Melinda Roy; José N Onuchic; Shachi Gosavi; Patricia A Jennings
Journal:  Proc Natl Acad Sci U S A       Date:  2012-01-17       Impact factor: 11.205

Review 4.  A review about nothing: are apolar cavities in proteins really empty?

Authors:  Brian W Matthews; Lijun Liu
Journal:  Protein Sci       Date:  2009-03       Impact factor: 6.725

5.  Water in the polar and nonpolar cavities of the protein interleukin-1β.

Authors:  Hao Yin; Guogang Feng; G Marius Clore; Gerhard Hummer; Jayendran C Rasaiah
Journal:  J Phys Chem B       Date:  2010-11-03       Impact factor: 2.991

6.  Determination of solvent content in cavities in IL-1beta using experimentally phased electron density.

Authors:  Michael L Quillin; Paul T Wingfield; Brian W Matthews
Journal:  Proc Natl Acad Sci U S A       Date:  2006-12-18       Impact factor: 11.205

7.  Quantum-mechanics-derived 13Calpha chemical shift server (CheShift) for protein structure validation.

Authors:  Jorge A Vila; Yelena A Arnautova; Osvaldo A Martin; Harold A Scheraga
Journal:  Proc Natl Acad Sci U S A       Date:  2009-09-08       Impact factor: 11.205

8.  Automatic recognition of hydrophobic clusters and their correlation with protein folding units.

Authors:  M H Zehfus
Journal:  Protein Sci       Date:  1995-06       Impact factor: 6.725

9.  Identification of compact, hydrophobically stabilized domains and modules containing multiple peptide chains.

Authors:  M H Zehfus
Journal:  Protein Sci       Date:  1997-06       Impact factor: 6.725

10.  Protein backbone angle restraints from searching a database for chemical shift and sequence homology.

Authors:  G Cornilescu; F Delaglio; A Bax
Journal:  J Biomol NMR       Date:  1999-03       Impact factor: 2.835

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