Raptor protein contains a caspase-like domain

被引：20

作者：

Ginalski, K

Zhang, H

Grishin, NV

机构：

[1] Univ Texas, SW Med Ctr, Dept Biochem, Dallas, TX 75390 USA

[2] BioInfoBank Inst, PL-60744 Poznan, Poland

[3] Univ Texas, SW Med Ctr, Howard Hughes Med Inst, Dallas, TX 75390 USA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2004年 / 29卷 / 10期

关键词：

D O I：

10.1016/j.tibs.2004.08.006

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Using state-of-the-art sequence analysis and structure-prediction methods a caspase-like domain in the N-terminal region of raptor proteins has been identified. This domain, which is characterized by the presence of invariant catalytic Cys-His dyad, is evolutionarily and structurally related to known caspases and might have protease activity. This finding suggests several unexpected aspects of raptor function in the target of rapamycin (TOR) signaling pathway.

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收藏

页码：522 / 524

页数：3

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