This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3lkx

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 04:24, 5 August 2016

Human nac dimerization domain

Structural highlights

3lkx is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	NACA (HUMAN), BTF3 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

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.

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.

References

↑ Moller I, Beatrix B, Kreibich G, Sakai H, Lauring B, Wiedmann M. Unregulated exposure of the ribosomal M-site caused by NAC depletion results in delivery of non-secretory polypeptides to the Sec61 complex. FEBS Lett. 1998 Dec 11;441(1):1-5. PMID:9877153
↑ Beatrix B, Sakai H, Wiedmann M. The alpha and beta subunit of the nascent polypeptide-associated complex have distinct functions. J Biol Chem. 2000 Dec 1;275(48):37838-45. PMID:10982809 doi:10.1074/jbc.M006368200
↑ Lopez S, Stuhl L, Fichelson S, Dubart-Kupperschmitt A, St Arnaud R, Galindo JR, Murati A, Berda N, Dubreuil P, Gomez S. NACA is a positive regulator of human erythroid-cell differentiation. J Cell Sci. 2005 Apr 15;118(Pt 8):1595-605. Epub 2005 Mar 22. PMID:15784678 doi:jcs.02295
↑ 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. 2010 Mar 16. PMID:20214399 doi:10.1021/bi902050p

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3lkx"

@@ Line 1: / Line 1: @@
 ==Human nac dimerization domain==
 <StructureSection load='3lkx' size='340' side='right' caption='[[3lkx]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[3lkx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LKX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LKX FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NACA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), BTF3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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>
+<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://pdbe.org/3lkx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lkx RCSB], [http://www.ebi.ac.uk/pdbsum/3lkx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lkx ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lkx ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 26: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3lkx" style="background-color:#fffaf0;"></div>
 ==See Also==

3lkx

From Proteopedia

Revision as of 04:24, 5 August 2016

Human nac dimerization domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox