4oh9
From Proteopedia
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| - | ''' | + | ==Crystal Structure of the human MST2 SARAH homodimer== |
| + | <StructureSection load='4oh9' size='340' side='right' caption='[[4oh9]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4oh9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OH9 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oh8|4oh8]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oh9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oh9 RCSB], [http://www.ebi.ac.uk/pdbsum/4oh9 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Despite recent progress in research on the Hippo signalling pathway, the structural information available in this area is extremely limited. Intriguingly, the homodimeric and heterodimeric interactions of mammalian sterile 20-like (MST) kinases through the so-called `SARAH' (SAV/RASSF/HPO) domains play a critical role in cellular homeostasis, dictating the fate of the cell regarding cell proliferation or apoptosis. To understand the mechanism of the heterodimerization of SARAH domains, the three-dimensional structures of an MST1-RASSF5 SARAH heterodimer and an MST2 SARAH homodimer were determined by X-ray crystallography and were analysed together with that previously determined for the MST1 SARAH homodimer. While the structure of the MST2 homodimer resembled that of the MST1 homodimer, the MST1-RASSF5 heterodimer showed distinct structural features. Firstly, the six N-terminal residues (Asp432-Lys437), which correspond to the short N-terminal 310-helix h1 kinked from the h2 helix in the MST1 homodimer, were disordered. Furthermore, the MST1 SARAH domain in the MST1-RASSF5 complex showed a longer helical structure (Ser438-Lys480) than that in the MST1 homodimer (Val441-Lys480). Moreover, extensive polar and nonpolar contacts in the MST1-RASSF5 SARAH domain were identified which strengthen the interactions in the heterodimer in comparison to the interactions in the homodimer. Denaturation experiments performed using urea also indicated that the MST-RASSF heterodimers are substantially more stable than the MST homodimers. These findings provide structural insights into the role of the MST1-RASSF5 SARAH domain in apoptosis signalling. | ||
| - | + | Structural basis of the heterodimerization of the MST and RASSF SARAH domains in the Hippo signalling pathway.,Hwang E, Cheong HK, Mushtaq AU, Kim HY, Yeo KJ, Kim E, Lee WC, Hwang KY, Cheong C, Jeon YH Acta Crystallogr D Biol Crystallogr. 2014 Jul 1;70(Pt 7):1944-53. doi:, 10.1107/S139900471400947X. Epub 2014 Jun 29. PMID:25004971<ref>PMID:25004971</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Non-specific serine/threonine protein kinase]] | ||
| + | [[Category: Cheong, C.]] | ||
| + | [[Category: Cheong, H K.]] | ||
| + | [[Category: Hwang, E.]] | ||
| + | [[Category: Hwang, K Y.]] | ||
| + | [[Category: Jeon, Y H.]] | ||
| + | [[Category: Kim, E.]] | ||
| + | [[Category: Kim, H Y.]] | ||
| + | [[Category: Lee, W C.]] | ||
| + | [[Category: Mushtaq, A Ul.]] | ||
| + | [[Category: Yeo, K J.]] | ||
| + | [[Category: Coiled-coil]] | ||
| + | [[Category: Heterodimerization]] | ||
| + | [[Category: Homodierizarion]] | ||
| + | [[Category: Sarah domain]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 07:51, 23 July 2014
Crystal Structure of the human MST2 SARAH homodimer
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