3LKX

Human nac dimerization domain

Summary for 3LKX

• Entry DOI: 10.2210/pdb3lkx/pdb
• Descriptor: Transcription factor BTF3, Nascent polypeptide-associated complex subunit alpha (3 entities in total)
• Functional Keywords: beta-barrel, chaperone
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm : P20290 Q13765
• Total number of polymer chains: 2
• Total formula weight: 13137.83

Authors

Liu, Y.,Hu, Y.,Li, X.,Niu, L.,Teng, M. (deposition date: 2010-01-28, release date: 2010-03-23, Last modification date: 2023-11-01)

Primary citation

Liu, Y.,Hu, Y.,Li, X.,Niu, L.,Teng, M.
The crystal structure of the human nascent polypeptide-associated complex domain reveals a nucleic acid-binding region on the NACA subunit
Biochemistry, 49:2890-2896, 2010

PubMed Abstract: In archaea and eukaryotes, the nascent polypeptide-associated complex (NAC) is one of the cytosolic chaperones that contact the nascent polypeptide chains as they emerge from the ribosome and assist in post-translational processes. The eukaryotic NAC is a heterodimer, and its two subunits form a stable complex through a dimerizing domain called the NAC domain. In addition to acting as a protein translation chaperone, the NAC subunits also function individually in transcriptional regulation. Here we report the crystal structure of the human NAC domain, which reveals the manner of human NAC dimerization. On the basis of the structure, we identified a region in the NAC domain of the human NAC alpha-subunit as a new nucleic acid-binding region, which is blocked from binding nucleic acids in the heterodimeric complex by a helix region in the beta-subunit.

PubMed: 20214399
DOI: 10.1021/bi902050p

Experimental method

X-RAY DIFFRACTION (2.5 Å)