It Takes Two Binding Sites for Calcineurin and NFAT to Tango

被引：10
|
作者：
Liu, Jun O. [1 ,2 ]
Nacev, Benjamin A. [1 ,3 ]
Xu, Jing [1 ]
Bhat, Shridhar [1 ]
机构：
[1] Johns Hopkins Sch Med, Dept Pharmacol, Baltimore, MD 21205 USA
[2] Johns Hopkins Sch Med, Dept Oncol, Baltimore, MD 21205 USA
[3] Johns Hopkins Sch Med, Med Scientist Training Program, Baltimore, MD 21205 USA
来源：
MOLECULAR CELL | 2009年 / 33卷 / 06期
关键词：
CRYSTAL-STRUCTURE; CYCLOSPORINE-A; CYCLOPHILIN; INHIBITION; ACTIVATION; COMPLEXES; COMMON;
D O I：
10.1016/j.molcel.2009.03.005
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：
In a recent issue of Molecular Cell, Rodriguez et al. (2009) identified the NFAT LxVP motif binding site as the same composite surface formed by the two calcineurin subunits that is recognized by the cyclophilin-CsA and FKBP-FK506 complexes.
引用
收藏
页码：676 / 678
页数：3
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