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4i1b
From Proteopedia
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'''FUNCTIONAL IMPLICATIONS OF INTERLEUKIN-1BETA BASED ON THE THREE-DIMENSIONAL STRUCTURE''' | '''FUNCTIONAL IMPLICATIONS OF INTERLEUKIN-1BETA BASED ON THE THREE-DIMENSIONAL STRUCTURE''' | ||
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[[Category: Svensson, L A.]] | [[Category: Svensson, L A.]] | ||
[[Category: Veerapandian, B.]] | [[Category: Veerapandian, B.]] | ||
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Revision as of 19:25, 4 May 2008
FUNCTIONAL IMPLICATIONS OF INTERLEUKIN-1BETA BASED ON THE THREE-DIMENSIONAL STRUCTURE
Overview
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.
About this Structure
4I1B is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Functional implications of interleukin-1 beta based on the three-dimensional structure., Veerapandian B, Gilliland GL, Raag R, Svensson AL, Masui Y, Hirai Y, Poulos TL, Proteins. 1992 Jan;12(1):10-23. PMID:1553379 Page seeded by OCA on Sun May 4 22:25:31 2008
