3vyc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:43, 20 March 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Crystal structure of unliganded Saccharomyces cerevisiae CRM1 (Xpo1p)==
==Crystal structure of unliganded Saccharomyces cerevisiae CRM1 (Xpo1p)==
-
<StructureSection load='3vyc' size='340' side='right' caption='[[3vyc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+
<StructureSection load='3vyc' size='340' side='right'caption='[[3vyc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3vyc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VYC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VYC FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3vyc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VYC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VYC FirstGlance]. <br>
-
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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]] 2.1&#8491;</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=3vyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vyc OCA], [http://pdbe.org/3vyc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vyc RCSB], [http://www.ebi.ac.uk/pdbsum/3vyc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vyc 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=3vyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vyc OCA], [https://pdbe.org/3vyc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vyc RCSB], [https://www.ebi.ac.uk/pdbsum/3vyc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vyc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/XPO1_YEAST XPO1_YEAST]] Receptor for the leucine-rich nuclear export signal (NES).
+
[https://www.uniprot.org/uniprot/XPO1_YEAST XPO1_YEAST] Receptor for the leucine-rich nuclear export signal (NES).
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
CRM1 mediates nuclear export of numerous proteins and ribonucleoproteins containing a leucine-rich nuclear export signal (NES). Binding of RanGTP to CRM1 in the nucleus stabilizes cargo association with CRM1, and vice versa, but the mechanism underlying the positive cooperativity in RanGTP and NES binding to CRM1 remains incompletely understood. Herein we report a 2.1-A-resolution crystal structure of unliganded Saccharomyces cerevisiae CRM1 (Xpo1p) that demonstrates that an internal loop of CRM1 (referred to as HEAT9 loop) is primarily responsible for maintaining the NES-binding cleft in a closed conformation, rendering CRM1 incapable of NES binding in the absence of RanGTP. The structure also shows that the C-terminal tail of CRM1 stabilizes the autoinhibitory conformation of the HEAT9 loop and thereby reinforces autoinhibition. Comparison with the structures of CRM1-NES-RanGTP complexes reveals how binding of RanGTP is associated with a series of allosteric conformational changes in CRM1 that lead to opening of the NES-binding cleft, allowing for stable binding of NES cargoes.
+
-
 
+
-
A 2.1-A-resolution crystal structure of unliganded CRM1 reveals the mechanism of autoinhibition.,Saito N, Matsuura Y J Mol Biol. 2013 Jan 23;425(2):350-64. doi: 10.1016/j.jmb.2012.11.014. Epub 2012 , Nov 16. PMID:23164569<ref>PMID:23164569</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3vyc" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
-
*[[Exportin|Exportin]]
+
*[[Exportin 3D structures|Exportin 3D structures]]
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Baker's yeast]]
+
[[Category: Large Structures]]
-
[[Category: Matsuura, Y]]
+
[[Category: Saccharomyces cerevisiae S288C]]
-
[[Category: Saito, N]]
+
[[Category: Matsuura Y]]
-
[[Category: Heat repeat]]
+
[[Category: Saito N]]
-
[[Category: Nuclear export]]
+
-
[[Category: Protein transport]]
+

Current revision

Crystal structure of unliganded Saccharomyces cerevisiae CRM1 (Xpo1p)

PDB ID 3vyc

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3vyc"
Personal tools