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Article

Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening.

Molecular cell - 12 Mar 2010

Sadre-Bazzaz Kianoush, Whitby Frank G, Robinson Howard, Formosa Tim, Hill Christopher P

Abstract excerpt

The proteasome is an abundant protease that is critically important for numerous cellular pathways. Proteasomes are activated in vitro by three known classes of proteins/complexes, including Blm10/PA200. Here, we report a 3.4 A resolution crystal structure of a proteasome-Blm10 complex, which rev...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 20227375
DOI: 10.1016/j.molcel.2010.02.002
PMCID: PMC2859072

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-20227375-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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