View source for 5dh9


==Crystal Structure of PKI NES Flip Mutant Peptide in complex with CRM1-Ran-RanBP1==
<StructureSection load='5dh9' size='340' side='right'caption='[[5dh9]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5dh9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [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=5DH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DH9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=5dh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dh9 OCA], [https://pdbe.org/5dh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dh9 RCSB], [https://www.ebi.ac.uk/pdbsum/5dh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dh9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IPKA_HUMAN IPKA_HUMAN] Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Chromosome Region of Maintenance 1 (CRM1) protein mediates nuclear export of hundreds of proteins through recognition of their nuclear export signals (NESs), which are highly variable in sequence and structure. The plasticity of the CRM1-NES interaction is not well understood, as there are many NES sequences that seem incompatible with structures of the NES-bound CRM1 groove. Crystal structures of CRM1 bound to two different NESs with unusual sequences showed the NES peptides binding the CRM1 groove in the opposite orientation (minus) to that of previously studied NESs (plus). Comparison of minus and plus NESs identified structural and sequence determinants for NES orientation. The binding of NESs to CRM1 in both orientations results in a large expansion in NES consensus patterns and therefore a corresponding expansion of potential NESs in the proteome.

Structural determinants of nuclear export signal orientation in binding to exportin CRM1.,Fung HY, Fu SC, Brautigam CA, Chook YM Elife. 2015 Sep 8;4. doi: 10.7554/eLife.10034. PMID:26349033<ref>PMID:26349033</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5dh9" style="background-color:#fffaf0;"></div>

==See Also==
*[[Exportin 3D structures|Exportin 3D structures]]
*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Chook YM]]
[[Category: Fung HY]]