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

Lanfeng Wang, Wenchi Zhang, Lu Wang, Xuejun C. Zhang, Xuemei Li, Zihe Rao

Research output: Contribution to journalArticlepeer-review


Nascent polypeptide associated complex (NAC) and its two isolated subunits, αNAC and βNAC, play important roles in nascent peptide targeting. We determined a 1.9 Å resolution crystal structure of the interaction core of NAC heterodimer and a 2.4 Å resolution crystal structure of αNAC 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 structure-function relationship of NAC.

Original languageEnglish (US)
Pages (from-to)406-416
Number of pages11
JournalProtein and Cell
Issue number4
StatePublished - Apr 2010
Externally publishedYes


  • crystal structure
  • nascent polypeptide-associated complex
  • αNAC homodimer
  • βNAC

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Drug Discovery
  • Cell Biology


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