3lkx: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lkx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lkx RCSB], [http://www.ebi.ac.uk/pdbsum/3lkx PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lkx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lkx RCSB], [http://www.ebi.ac.uk/pdbsum/3lkx PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/BTF3_HUMAN BTF3_HUMAN]] General transcription factor. BTF3 can form a stable complex with RNA polymerase II. Required for the initiation of transcription. [[http://www.uniprot.org/uniprot/NACA_HUMAN NACA_HUMAN]] Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites). May act as a specific coactivator for JUN, binding to DNA and stabilizing the interaction of JUN homodimers with target gene promoters.<ref>PMID:9877153</ref> <ref>PMID:10982809</ref> <ref>PMID:15784678</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 18:47, 25 December 2014
Human nac dimerization domainHuman nac dimerization domain
Structural highlights
Function[BTF3_HUMAN] General transcription factor. BTF3 can form a stable complex with RNA polymerase II. Required for the initiation of transcription. [NACA_HUMAN] Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites). May act as a specific coactivator for JUN, binding to DNA and stabilizing the interaction of JUN homodimers with target gene promoters.[1] [2] [3] 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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