Structural biology of the PCI-protein fold

Andrew M Ellisdon; Murray Stewart

doi:10.4161/bioa.21131

Structural biology of the PCI-protein fold

Andrew M Ellisdon, Murray Stewart

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › Research › peer-review

33 Citations (Scopus)

Abstract

The PCI fold is based on a stack of alpha-helices topped with a winged-helix domain and is found in a range of proteins that form central parts of large complexes such as the proteasome lid, the COP9 signalosome, elongation factor eIF3, and the TREX-2 complex. Recent structural determinations have given intriguing insight into how these folds function both to facilitate the generation of larger proteinaceous assembles and also to interact functionally with nucleic acids.

Original language	English
Pages (from-to)	1 - 6
Number of pages	6
Journal	Bioarchitecture
Volume	2
Issue number	4
DOIs	https://doi.org/10.4161/bioa.21131
Publication status	Published - 2012

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10.4161/bioa.21131

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Structural biology of the PCI-protein fold

Abstract

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