Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats

Kobe, Bostjan and Deisenhofer, Johann (1993) Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats. Nature, 366 6457: 751-756. doi:10.1038/366751a0


Author Kobe, Bostjan
Deisenhofer, Johann
Title Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats
Journal name Nature   Check publisher's open access policy
ISSN 0028-0836
1476-4687
Publication date 1993
Sub-type Article (original research)
DOI 10.1038/366751a0
Volume 366
Issue 6457
Start page 751
End page 756
Total pages 6
Place of publication London, UK
Publisher Nature Publishing Group
Language eng
Subject 060112 Structural Biology (incl. Macromolecular Modelling)
Formatted abstract
RIBONUCLEASE inhibitor is a cytoplasmic protein that tightly binds and inhibits ribonucleases of the pancreatic ribonuclease super-family1. The primary sequence of this inhibitor contains leucine-rich repeats (LRRs); these motifs are present in many proteins that participate in protein–protein interactions and have different functions and cellular locations. In vivo, ribonuclease inhibitor may have a role in the regulation of RNA turnover in mammalian cells and in angiogenesis. To define the structural features of LRR proteins and to understand better the nature of the tight interaction of ribonuclease inhibitor with ribonucleases, we have determined the crystal structure of the porcine inhibitor. To our knowledge, this is the first three-dimensional structure of a protein containing LRRs and represents a new class of α/ ß protein fold. Individual repeats constitute β–α structural units that probably also occur in other proteins containing LRRs. The non-globular shape of the structure and the exposed face of the parallel β-sheet may explain why LRRs are used to achieve strong protein–protein interactions. A possible ribonuclease-binding region incorporates the surface formed by the parallel ß-sheet and the betaalpha loops.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
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Created: Tue, 20 Jul 2010, 16:01:21 EST by Laura McTaggart on behalf of Faculty of Science