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| | ==Mammalian SCAN domain dimer is a domain-swapped homologue of the HIV capsid C-terminal domain== | | ==Mammalian SCAN domain dimer is a domain-swapped homologue of the HIV capsid C-terminal domain== |
| - | <StructureSection load='1y7q' size='340' side='right'caption='[[1y7q]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1y7q' size='340' side='right'caption='[[1y7q]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1y7q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y7Q OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Y7Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1y7q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y7Q FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ZNF174, ZSCAN8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1y7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y7q OCA], [http://pdbe.org/1y7q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y7q RCSB], [http://www.ebi.ac.uk/pdbsum/1y7q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y7q ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1y7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y7q OCA], [https://pdbe.org/1y7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y7q RCSB], [https://www.ebi.ac.uk/pdbsum/1y7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y7q ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ZN174_HUMAN ZN174_HUMAN]] Transcriptional repressor.<ref>PMID:7673192</ref> | + | [https://www.uniprot.org/uniprot/ZN174_HUMAN ZN174_HUMAN] Transcriptional repressor.<ref>PMID:7673192</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Collins, T]] | + | [[Category: Collins T]] |
| - | [[Category: Ivanov, D]] | + | [[Category: Ivanov D]] |
| - | [[Category: Maki, J L]] | + | [[Category: Maki JL]] |
| - | [[Category: Stone, J R]] | + | [[Category: Stone JR]] |
| - | [[Category: Wagner, G]] | + | [[Category: Wagner G]] |
| - | [[Category: C2h2 zinc finger associated]]
| + | |
| - | [[Category: Dimer]]
| + | |
| - | [[Category: Retroviral capsid c-terminal domain]]
| + | |
| - | [[Category: Scan domain]]
| + | |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
ZN174_HUMAN Transcriptional repressor.[1]
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
Retroviral assembly is driven by multiple interactions mediated by the Gag polyprotein, the main structural component of the forming viral shell. Critical determinants of Gag oligomerization are contained within the C-terminal domain (CTD) of the capsid protein, which also harbors a conserved sequence motif, the major homology region (MHR), in the otherwise highly variable Gag. An unexpected clue about the MHR function in retroviral assembly emerges from the structure of the zinc finger-associated SCAN domain we describe here. The SCAN dimer adopts a fold almost identical to that of the retroviral capsid CTD but uses an entirely different dimerization interface caused by swapping the MHR-like element between the monomers. Mutations in retroviral capsid proteins and functional data suggest that a SCAN-like MHR-swapped CTD dimer forms during immature particle assembly. In the SCAN-like dimer, the MHR contributes the major part of the large intertwined dimer interface explaining its functional significance.
Mammalian SCAN domain dimer is a domain-swapped homolog of the HIV capsid C-terminal domain.,Ivanov D, Stone JR, Maki JL, Collins T, Wagner G Mol Cell. 2005 Jan 7;17(1):137-43. PMID:15629724[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Williams AJ, Khachigian LM, Shows T, Collins T. Isolation and characterization of a novel zinc-finger protein with transcription repressor activity. J Biol Chem. 1995 Sep 22;270(38):22143-52. PMID:7673192
- ↑ Ivanov D, Stone JR, Maki JL, Collins T, Wagner G. Mammalian SCAN domain dimer is a domain-swapped homolog of the HIV capsid C-terminal domain. Mol Cell. 2005 Jan 7;17(1):137-43. PMID:15629724 doi:10.1016/j.molcel.2004.12.015
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