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| | ==Crystal structure of human nuclear migration protein NudC== | | ==Crystal structure of human nuclear migration protein NudC== |
| - | <StructureSection load='3qor' size='340' side='right' caption='[[3qor]], [[Resolution|resolution]] 1.75Å' scene=''> | + | <StructureSection load='3qor' size='340' side='right'caption='[[3qor]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3qor]] is a 5 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=3QOR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QOR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3qor]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QOR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> |
| | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr> | | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NUDC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NUDC ([https://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=3qor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qor OCA], [http://pdbe.org/3qor PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qor RCSB], [http://www.ebi.ac.uk/pdbsum/3qor PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qor 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=3qor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qor OCA], [https://pdbe.org/3qor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qor RCSB], [https://www.ebi.ac.uk/pdbsum/3qor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qor ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NUDC_HUMAN NUDC_HUMAN]] Plays a role in neurogenesis and neuronal migration (By similarity). Necessary for correct formation of mitotic spindles and chromosome separation during mitosis. Necessary for cytokinesis and cell proliferation.<ref>PMID:12679384</ref> <ref>PMID:12852857</ref> | + | [[https://www.uniprot.org/uniprot/NUDC_HUMAN NUDC_HUMAN]] Plays a role in neurogenesis and neuronal migration (By similarity). Necessary for correct formation of mitotic spindles and chromosome separation during mitosis. Necessary for cytokinesis and cell proliferation.<ref>PMID:12679384</ref> <ref>PMID:12852857</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Human]] | | [[Category: Human]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Derewenda, U]] | | [[Category: Derewenda, U]] |
| | [[Category: Derewenda, Z]] | | [[Category: Derewenda, Z]] |
| Structural highlights
Function
[NUDC_HUMAN] Plays a role in neurogenesis and neuronal migration (By similarity). Necessary for correct formation of mitotic spindles and chromosome separation during mitosis. Necessary for cytokinesis and cell proliferation.[1] [2]
Publication Abstract from PubMed
The NudC family consists of four conserved proteins with representatives in all eukaryotes. The archetypal nudC gene from Aspergillus nidulans is a member of the nud gene family that is involved in the maintenance of nuclear migration. This family also includes nudF, whose human orthologue, Lis1, codes for a protein essential for brain cortex development. Three paralogues of NudC are known in vertebrates: NudC, NudC-like (NudCL), and NudC-like 2 (NudCL2). The fourth distantly related member of the family, CML66, contains a NudC-like domain. The three principal NudC proteins have no catalytic activity but appear to play as yet poorly defined roles in proliferating and dividing cells. We present crystallographic and NMR studies of the human NudC protein and discuss the results in the context of structures recently deposited by structural genomics centers (i.e., NudCL and mouse NudCL2). All proteins share the same core CS domain characteristic of proteins acting either as cochaperones of Hsp90 or as independent small heat shock proteins. However, while NudC and NudCL dimerize via an N-terminally located coiled coil, the smaller NudCL2 lacks this motif and instead dimerizes as a result of unique domain swapping. We show that NudC and NudCL, but not NudCL2, inhibit the aggregation of several target proteins, consistent with an Hsp90-independent heat shock protein function. Importantly, and in contrast to several previous reports, none of the three proteins is able to form binary complexes with Lis1. The availability of structural information will be of help in further studies on the cellular functions of the NudC family.
Structural Features and Chaperone Activity of the NudC Protein Family.,Zheng M, Cierpicki T, Burdette AJ, Utepbergenov D, Janczyk PL, Derewenda U, Stukenberg PT, Caldwell KA, Derewenda ZS J Mol Biol. 2011 Jun 24;409(5):722-41. Epub 2011 Apr 21. PMID:21530541[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Aumais JP, Williams SN, Luo W, Nishino M, Caldwell KA, Caldwell GA, Lin SH, Yu-Lee LY. Role for NudC, a dynein-associated nuclear movement protein, in mitosis and cytokinesis. J Cell Sci. 2003 May 15;116(Pt 10):1991-2003. Epub 2003 Apr 1. PMID:12679384 doi:http://dx.doi.org/10.1242/jcs.00412
- ↑ Zhou T, Aumais JP, Liu X, Yu-Lee LY, Erikson RL. A role for Plk1 phosphorylation of NudC in cytokinesis. Dev Cell. 2003 Jul;5(1):127-38. PMID:12852857
- ↑ Zheng M, Cierpicki T, Burdette AJ, Utepbergenov D, Janczyk PL, Derewenda U, Stukenberg PT, Caldwell KA, Derewenda ZS. Structural Features and Chaperone Activity of the NudC Protein Family. J Mol Biol. 2011 Jun 24;409(5):722-41. Epub 2011 Apr 21. PMID:21530541 doi:10.1016/j.jmb.2011.04.018
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