Crystal structure of a mycobacterial Insig homolog provides insight into how these sensors monitor sterol levels | Zendy

Ruobing Ren | Zendy; Xinhui Zhou | Zendy; Yuan He | Zendy; Meng Ke | Zendy; Jianping Wu | Zendy; Xiaohui Liu | Zendy; Chuangye Yan | Zendy; Yixuan Wu | Zendy; Xin Gong | Zendy; Xiaoguang Lei | Zendy; S. Frank Yan | Zendy; Arun Radhakrishnan | Zendy; Nieng Yan | Zendy

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Crystal structure of a mycobacterial Insig homolog provides insight into how these sensors monitor sterol levels

Author(s) -

Ruobing Ren,

Xinhui Zhou,

Yuan He,

Meng Ke,

Jianping Wu,

Xiaohui Liu,

Chuangye Yan,

Yixuan Wu,

Xin Gong,

Xiaoguang Lei,

S. Frank Yan,

Arun Radhakrishnan,

Nieng Yan

Publication year - 2015

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.aab1091

Subject(s) - endoplasmic reticulum , sterol , sterol regulatory element binding protein , microbiology and biotechnology , biology , biochemistry , cholesterol

Structure of a sterol sensor The aberrant accumulation of sterols contributes to heart attack and stroke. Two proteins embedded in the membrane of the endoplasmic reticulum, Insig-1 and Insig-2, are key players in the cellular pathway that regulates cellular sterol levels. Renet al. report the structure of a mycobacterial homolog of Insig. The structure, together with biochemical experiments, suggests how Insig interacts with other components of the sterol regulatory pathway.Science , this issue p.187

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