5h1x: Difference between revisions
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The | ==Crystal Structure of rat Nup62 Coiled-coil motif== | ||
<StructureSection load='5h1x' size='340' side='right' caption='[[5h1x]], [[Resolution|resolution]] 2.41Å' scene=''> | |||
== 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 [http://oca.weizmann.ac.il/oca-docs/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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5h1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h1x OCA], [http://pdbe.org/5h1x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h1x RCSB], [http://www.ebi.ac.uk/pdbsum/5h1x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h1x ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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;"> | |||
== Publication Abstract from PubMed == | |||
The 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<ref>PMID:28406021</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 5h1x" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
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</StructureSection> | |||
[[Category: Pravin, D]] | |||
[[Category: Coiled-coil]] | |||
[[Category: Structural protein]] | |||