View source for 6p2u


==Structure of Mortalin-NBD with N6-propargyladenosine-5'-diphosphate==
<StructureSection load='6p2u' size='340' side='right'caption='[[6p2u]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6p2u]] 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=6P2U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P2U 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO7:9-{5-O-[(S)-hydroxy(phosphonooxy)phosphoryl]-alpha-D-ribofuranosyl}-N-(prop-2-yn-1-yl)-9H-purin-6-amine'>NO7</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=6p2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p2u OCA], [https://pdbe.org/6p2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p2u RCSB], [https://www.ebi.ac.uk/pdbsum/6p2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p2u ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GRP75_HUMAN GRP75_HUMAN] Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Our early efforts to find a covalent inhibitor of mortalin, a member of the 70 kD heat shock protein (Hsp70) family, led us to solve the structure of the mortalin nucleotide-binding domain (NBD) in complex with N6-propargyladenosine-5'-diphosphate. The acquired structure emphasizes the ability of the nucleotide-binding pocket to accommodate modified ADP compounds. A library of ADP analogues modified at either the 2- or N6-positions of adenosine were screened against the mortalin-NBD. Competitive inhibition and binding assays of the analogues demonstrate that modifications at the 2- or N6-positions have potential to bind and inhibit mortalin uniquely compared to other Hsp70 homologs, and that modifications at the 2-position confer the greatest selectivity in binding and inhibition of the mortalin-NBD. This article is protected by copyright. All rights reserved.

2- and N6-Functionalized Adenosine-5'-diphosphate Analogues for the Inhibition of Mortalin.,Moseng MA, Nix JC, Page RC FEBS Lett. 2019 Jun 8. doi: 10.1002/1873-3468.13475. PMID:31177526<ref>PMID:31177526</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6p2u" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Moseng MA]]
[[Category: Page RC]]