5h1x: Difference between revisions
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==Crystal Structure of rat Nup62 Coiled-coil motif== | ==Crystal Structure of rat Nup62 Coiled-coil motif== | ||
<StructureSection load='5h1x' size='340' side='right' caption='[[5h1x]], [[Resolution|resolution]] 2.41Å' scene=''> | <StructureSection load='5h1x' size='340' side='right'caption='[[5h1x]], [[Resolution|resolution]] 2.41Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5h1x]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H1X OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5h1x]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H1X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H1X FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.41Å</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=5h1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h1x OCA], [https://pdbe.org/5h1x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h1x RCSB], [https://www.ebi.ac.uk/pdbsum/5h1x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h1x ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/NUP62_RAT NUP62_RAT] Essential component of the nuclear pore complex. The N-terminal is probably involved in nucleocytoplasmic transport. The C-terminal is probably involved in protein-protein interaction via coiled-coil formation and may function in anchorage of p62 to the pore complex. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5h1x" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5h1x" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Nucleoporin 3D structures|Nucleoporin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rattus norvegicus]] | ||
[[Category: | [[Category: Pravin D]] | ||
Latest revision as of 10:21, 9 August 2023
Crystal Structure of rat Nup62 Coiled-coil motifCrystal Structure of rat Nup62 Coiled-coil motif
Structural highlights
FunctionNUP62_RAT Essential component of the nuclear pore complex. The N-terminal is probably involved in nucleocytoplasmic transport. The C-terminal is probably involved in protein-protein interaction via coiled-coil formation and may function in anchorage of p62 to the pore complex. Publication Abstract from PubMedThe central transport channel of the vertebrate nuclear pore complex (NPC) consists of nucleoporins: Nup62, Nup54, and Nup58. The coiled-coil domains in alpha-helical regions of these nucleoporins are thought to be crucial for several protein-protein interactions in the NPC subcomplexes. In this study, we determined the crystal structure of the coiled-coil domain of rat Nup62 fragment (residues 362-425) to 2.4 A resolution. The crystal structure shows the conserved coiled-coil domain as a parallel three-helix bundle for the Nup62(362-425) fragment. On the basis of our size exclusion chromatography coupled to multiangle light scattering analysis and glutaraldehyde cross-linking experiments, we conclude that the Nup62(362-425) fragment displays dynamic behavior in solution and can also exist in either homodimeric or homotrimeric states. Our comparative analysis of the rat Nup62(362-425) homotrimeric structure with previously reported heterotrimeric structures [rat Nup62(362-425).Nup54(346-407) and Xenopus Nup62(358-485).Nup54(315-450).Nup58(283-406) complexes] demonstrates the structural basis for parallel triple-helix bundle formation for Nup62 with different partners. Moreover, we show that the coiled-coil domain of Nup62 is sufficient for interaction with the coiled-coil domain of rat Exo70, a protein in an exocyst complex. On the basis of these observations, we suggest the plausible chain replacement mechanism that yields to diverse protein assemblies with Nup62. In summary, the coiled-coil motif present in Nup62 imparts the ability to form a homotrimer and heterotrimers either with Nup54 or with Nup54-Nup58 within the NPCs as well as with Exo70 beyond the NPCs. These complexes of Nup62 suggest the crucial role of the coiled-coil motifs in providing plasticity to various modular assemblies. The Nup62 Coiled-Coil Motif Provides Plasticity for Triple-Helix Bundle Formation.,Dewangan PS, Sonawane PJ, Chouksey AR, Chauhan R Biochemistry. 2017 Jun 6;56(22):2803-2811. doi: 10.1021/acs.biochem.6b01050. Epub, 2017 Apr 26. PMID:28406021[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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