Functional implications of interleukin-1β based on the three-dimensional structure
| Autor: | Thomas L. Poulos, Anders L. Svensson, Yoshikatsu Hirai, Yoshihiro Masui, Reetta Raag, B. Veerapandian, Gary L. Gilliland |
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| Rok vydání: | 1992 |
| Předmět: |
Models
Molecular Functional role Protein Conformation Stereochemistry Hydrogen Bonding Crystal structure Biology Antiparallel (biochemistry) Biochemistry Epitope Structure-Activity Relationship Molecular dynamics Structural Biology Mutation Humans Molecule Site-directed mutagenesis Receptor Molecular Biology Interleukin-1 |
| Zdroj: | Proteins: Structure, Function, and Genetics. 12:10-23 |
| ISSN: | 1097-0134 0887-3585 |
| DOI: | 10.1002/prot.340120103 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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