Structural highlights
FunctionBTF3_HUMAN General transcription factor. BTF3 can form a stable complex with RNA polymerase II. Required for the initiation of transcription. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn 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. The Crystal Structure of the Human Nascent Polypeptide-Associated Complex Domain Reveals a Nucleic Acid-Binding Region on the NACA Subunit .,Liu Y, Hu Y, Li X, Niu L, Teng M Biochemistry. 2010 Mar 16. PMID:20214399[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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