View source for 3lj8


==Crystal Structure of MKP-4==
<StructureSection load='3lj8' size='340' side='right'caption='[[3lj8]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3lj8]] 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=3LJ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LJ8 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]] 2.7&#8491;</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=3lj8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lj8 OCA], [https://pdbe.org/3lj8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lj8 RCSB], [https://www.ebi.ac.uk/pdbsum/3lj8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lj8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DUS9_HUMAN DUS9_HUMAN] Inactivates MAP kinases. Has a specificity for the ERK family.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Map kinase phosphatase 4 (MKP-4), which has been implicated in signalling pathways that negatively regulate glucose uptake, belongs to the dual-specificity phosphatase (DUSP) family. An inherent property of MKPs is an ability to undergo structural rearrangement, transitioning from a partially active to a fully active conformation. Here, a 2.7 A resolution crystal structure of the catalytic domain of MKP-4 (MKP-4C) is presented. It was determined that the MKP-4C structure seriously deviates from canonical conformations of DUSPs and this characteristic feature results in significant gaps between the catalytic core and several surrounding loops which are unique compared with other MKP counterparts that adopt an active conformation. Using virtual library screening, it was found that inhibitors bind to MKP-4C with high affinity near these gaps. Inhibitors that target other binding sites instead of the active site can be utilized to prevent transition to a fully active conformation. Compounds that are able to make contacts with these sites in MKP-4 would not only provide a beneficial increase in affinity but may also permit greater specificity relative to other protein tyrosine phosphatases.

Exploring binding sites other than the catalytic core in the crystal structure of the catalytic domain of MKP-4.,Jeong DG, Yoon TS, Jung SK, Park BC, Park H, Ryu SE, Kim SJ Acta Crystallogr D Biol Crystallogr. 2011 Jan;67(Pt 1):25-31. Epub 2010, Dec 16. PMID:21206059<ref>PMID:21206059</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3lj8" style="background-color:#fffaf0;"></div>

==See Also==
*[[MAP kinase phosphatase|MAP kinase phosphatase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Jeong DG]]
[[Category: Jung S-K]]
[[Category: Kim SJ]]
[[Category: Park HS]]
[[Category: Ryu SE]]
[[Category: Yoon TS]]