Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its αNAC subunit  

作　　者：Lanfeng Wang Wenchi Zhang Lu Wang Xuejun C.Zhang Xuemei Li Zihe Rao 

机构地区：[1]National Laboratory of Biomacromolecules,Institute of Biophysics,Chinese Academy of Sciences,15 Datun Road,Beijing 100101,China [2]Structure Biology Laboratory,Tsinghua University,Beijing 100084,China [3]Tianjin Key Laboratory of Protein Science,College of Life Sciences,Nankai University,Tianjin 300071,China

出　　处：《Protein & Cell》2010年第4期406-416,共11页蛋白质与细胞（英文版）

基　　金：This work was supported by the National Natural Science Foundation of China(grant No.30730022);the National Basic Research Program(973 Program)(grant Nos.2006CB806503 and 2007CB914304);the National Programs for High Technology Research and Development Program(863 Program)(grant Nos.2006AA02A322 and 2006AA020502);the CAS(China)grant KSCX2-YW-R-05 to Z.R.

摘　　要：Nascent polypeptide associated complex(NAC)and its two isolated subunits,αNAC and βNAC,play important roles in nascent peptide targeting.We determined a 1.9Åresolution crystal structure of the interaction core of NAC heterodimer and a 2.4Åresolution crystal structure ofαNAC NAC domain homodimer.These structures provide detailed information of NAC heterodimerization and αNAC homodimerization.We found that the NAC domains of αNAC and βNAC share very similar folding despite of their relative low identity of amino acid sequences.Furthermore,different electric charge distributions of the two subunits at the NAC interface provide an explanation to the observation that the heterodimer of NAC complex is more stable than the single subunit homodimer.In addition,we successfully built a βNAC NAC domain homodimer model based on homologous modeling,suggesting that NAC domain dimerization is a general property of the NAC family.These 3D structures allow further studies on structurefunction relationship of NAC.

关 键 词：nascent polypeptide-associated complex αNAC homodimer βNAC crystal structure 

分 类 号：R73[医药卫生—肿瘤]