http://purl.uniprot.org/citations/25004971 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/25004971 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
http://purl.uniprot.org/citations/25004971 | http://purl.org/dc/terms/identifier | "doi:10.1107/s139900471400947x"xsd:string |
http://purl.uniprot.org/citations/25004971 | http://purl.uniprot.org/core/author | "Kim E."xsd:string |
http://purl.uniprot.org/citations/25004971 | http://purl.uniprot.org/core/author | "Lee W.C."xsd:string |
http://purl.uniprot.org/citations/25004971 | http://purl.uniprot.org/core/author | "Hwang K.Y."xsd:string |
http://purl.uniprot.org/citations/25004971 | http://purl.uniprot.org/core/author | "Cheong C."xsd:string |
http://purl.uniprot.org/citations/25004971 | http://purl.uniprot.org/core/author | "Cheong H.K."xsd:string |
http://purl.uniprot.org/citations/25004971 | http://purl.uniprot.org/core/author | "Jeon Y.H."xsd:string |
http://purl.uniprot.org/citations/25004971 | http://purl.uniprot.org/core/author | "Kim H.Y."xsd:string |
http://purl.uniprot.org/citations/25004971 | http://purl.uniprot.org/core/author | "Yeo K.J."xsd:string |
http://purl.uniprot.org/citations/25004971 | http://purl.uniprot.org/core/author | "Hwang E."xsd:string |
http://purl.uniprot.org/citations/25004971 | http://purl.uniprot.org/core/author | "Ul Mushtaq A."xsd:string |
http://purl.uniprot.org/citations/25004971 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
http://purl.uniprot.org/citations/25004971 | http://purl.uniprot.org/core/name | "Acta Crystallogr D Biol Crystallogr"xsd:string |
http://purl.uniprot.org/citations/25004971 | http://purl.uniprot.org/core/pages | "1944-1953"xsd:string |
http://purl.uniprot.org/citations/25004971 | http://purl.uniprot.org/core/title | "Structural basis of the heterodimerization of the MST and RASSF SARAH domains in the Hippo signalling pathway."xsd:string |
http://purl.uniprot.org/citations/25004971 | http://purl.uniprot.org/core/volume | "70"xsd:string |
http://purl.uniprot.org/citations/25004971 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/25004971 |
http://purl.uniprot.org/citations/25004971 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/25004971 |
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