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

Abstract

Nascent polypeptide associated complex (NAC) and its two isolated subunits, aNAC and bNAC, play important roles in nascent peptide targeting. We determined a 1.9 ? resolution crystal structure of the interaction core of NAC heterodimer and a 2.4 ? resolution crystal structure of aNAC NAC domain homodimer. These structures provide detailed information of NAC heterodimerization and aNAC homodimerization. We found that the NAC domains of aNAC and bNAC 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 bNAC 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.

Keywords

nascent polypeptide-associated complex / aNAC homodimer / bNAC / crystal structure

References

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