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 

作者机构：National Laboratory of BiomacromoleculesInstitute of BiophysicsChinese Academy of Sciences15 Datun RoadBeijing 100101China Structure Biology LaboratoryTsinghua UniversityBeijing 100084China Tianjin Key Laboratory of Protein ScienceCollege of Life SciencesNankai UniversityTianjin 300071China 

出 版 物：《Protein & Cell》 (蛋白质与细胞（英文版）)

年 卷 期：2010年第1卷第4期

页      面：406-416页

核心收录：

学科分类：1002[医学-临床医学] 100214[医学-肿瘤学] 10[医学] 

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 

主　　题：nascent polypeptide-associated complex αNAC homodimer βNAC crystal structure 

摘      要：Nascent polypeptide associated complex(NAC)and its two isolated subunits,αNAC and βNAC,play important roles in nascent peptide *** determined a 1.9Åresolution crystal structure of the interaction core of NAC heterodimer and a 2.4Åresolution crystal structure ofαNAC NAC domain *** structures provide detailed information of NAC heterodimerization and αNAC *** found that the NAC domains of αNAC and βNAC share very similar folding despite of their relative low identity of amino acid ***,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 *** 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 *** 3D structures allow further studies on structurefunction relationship of NAC.