This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1xks
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='1xks' size='340' side='right'caption='[[1xks]], [[Resolution|resolution]] 2.35Å' scene=''> | <StructureSection load='1xks' size='340' side='right'caption='[[1xks]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1xks]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1xks]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XKS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XKS FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35Å</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=1xks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xks OCA], [https://pdbe.org/1xks PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xks RCSB], [https://www.ebi.ac.uk/pdbsum/1xks PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xks 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=1xks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xks OCA], [https://pdbe.org/1xks PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xks RCSB], [https://www.ebi.ac.uk/pdbsum/1xks PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xks ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/NU133_HUMAN NU133_HUMAN] Involved in poly(A)+ RNA transport.<ref>PMID:11684705</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 19: | Line 19: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xks ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xks ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Nucleocytoplasmic transport occurs through nuclear pore complexes (NPCs) whose complex architecture is generated from a set of only approximately 30 proteins, termed nucleoporins. Here, we explore the domain structure of Nup133, a nucleoporin in a conserved NPC subcomplex that is crucial for NPC biogenesis and is believed to form part of the NPC scaffold. We show that human Nup133 contains two domains: a COOH-terminal domain responsible for its interaction with its subcomplex through Nup107; and an NH2-terminal domain whose crystal structure reveals a seven-bladed beta-propeller. The surface properties and conservation of the Nup133 beta-propeller suggest it may mediate multiple interactions with other proteins. Other beta-propellers are predicted in a third of all nucleoporins. These and several other repeat-based motifs appear to be major elements of nucleoporins, indicating a level of structural repetition that may conceptually simplify the assembly and disassembly of this huge protein complex. | ||
| - | |||
| - | Structural and functional analysis of Nup133 domains reveals modular building blocks of the nuclear pore complex.,Berke IC, Boehmer T, Blobel G, Schwartz TU J Cell Biol. 2004 Nov 22;167(4):591-7. PMID:15557116<ref>PMID:15557116</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1xks" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| Line 35: | Line 26: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Berke | + | [[Category: Berke IC]] |
| - | [[Category: Blobel | + | [[Category: Blobel G]] |
| - | [[Category: Boehmer | + | [[Category: Boehmer T]] |
| - | [[Category: Schwartz | + | [[Category: Schwartz TU]] |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
The crystal structure of the N-terminal domain of Nup133 reveals a beta-propeller fold common to several nucleoporins
| |||||||||||
