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| | <StructureSection load='3nd2' size='340' side='right'caption='[[3nd2]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='3nd2' size='340' side='right'caption='[[3nd2]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3nd2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ND2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3ND2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3nd2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ND2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ND2 FirstGlance]. <br> |
| - | </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=3nd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nd2 OCA], [http://pdbe.org/3nd2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nd2 RCSB], [http://www.ebi.ac.uk/pdbsum/3nd2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nd2 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</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=3nd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nd2 OCA], [https://pdbe.org/3nd2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nd2 RCSB], [https://www.ebi.ac.uk/pdbsum/3nd2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nd2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/IMB1_YEAST IMB1_YEAST]] Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Serves a receptor for nuclear localization signals. Mediates the nuclear import of histones H2A and H2B.<ref>PMID:11309407</ref> | + | [https://www.uniprot.org/uniprot/IMB1_YEAST IMB1_YEAST] Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Serves a receptor for nuclear localization signals. Mediates the nuclear import of histones H2A and H2B.<ref>PMID:11309407</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: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Forwood, J K]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Kobe, B]] | + | [[Category: Forwood JK]] |
| - | [[Category: Importin]] | + | [[Category: Kobe B]] |
| - | [[Category: Karyopherin]]
| + | |
| - | [[Category: Nuclear import]]
| + | |
| - | [[Category: Nuclear transport]]
| + | |
| - | [[Category: Receptor]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
IMB1_YEAST Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Serves a receptor for nuclear localization signals. Mediates the nuclear import of histones H2A and H2B.[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
The structure of solenoid proteins facilitates a higher degree of flexibility than most folded proteins. In importin-beta, a nuclear import factor built from 19 tandem HEAT repeats, flexibility plays a crucial role in allowing interactions with a range of different partners. We present a comprehensive analysis of importin-beta flexibility based on a number of different approaches. We determined the crystal structure of unliganded Saccharomyces cerevisiae importin-beta (Kap95) to allow a quantitative comparison with importin-beta bound to different partners. Complementary mutagenesis, small angle X-ray scattering and molecular dynamics studies suggest that the protein samples several conformations in solution. The analyses suggest the flexibility of the solenoid is generated by cumulative small movements along its length. Importin-beta illustrates how solenoid proteins can orchestrate protein interactions in many cellular pathways.
Quantitative structural analysis of importin-beta flexibility: paradigm for solenoid protein structures.,Forwood JK, Lange A, Zachariae U, Marfori M, Preast C, Grubmuller H, Stewart M, Corbett AH, Kobe B Structure. 2010 Sep 8;18(9):1171-83. PMID:20826343[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mosammaparast N, Jackson KR, Guo Y, Brame CJ, Shabanowitz J, Hunt DF, Pemberton LF. Nuclear import of histone H2A and H2B is mediated by a network of karyopherins. J Cell Biol. 2001 Apr 16;153(2):251-62. PMID:11309407
- ↑ Forwood JK, Lange A, Zachariae U, Marfori M, Preast C, Grubmuller H, Stewart M, Corbett AH, Kobe B. Quantitative structural analysis of importin-beta flexibility: paradigm for solenoid protein structures. Structure. 2010 Sep 8;18(9):1171-83. PMID:20826343 doi:10.1016/j.str.2010.06.015
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