2jo8
From Proteopedia
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Solution structure of C-terminal domain of human mammalian sterile 20-like kinase 1 (MST1)
Overview
In eukaryotic cells, apoptosis and cell cycle arrest by the Ras --> RASSF, --> MST pathway are controlled by the interaction of SARAH (for, Salvador/Rassf/Hippo) domains in the C-terminal part of tumor suppressor, proteins. The Mst1 SARAH domain interacts with its homologous domain of, Rassf1 and Rassf5 (also known as Nore1) by forming a heterodimer that, mediates the apoptosis process. Here, we describe the homodimeric, structure of the human Mst1 SARAH domain and its heterotypic interaction, with the Rassf5 and Salvador (Sav) SARAH domain. The Mst1 SARAH structure, forms a homodimer containing two helices per monomer. An antiparallel, arrangement of the long alpha-helices (h2/h2') provides an elongated, binding interface between the two monomers, and the short 3(10) helices, (h1/h1') are folded toward that of the other monomer. Chemical shift, perturbation experiments identified an elongated, tight-binding interface, with the Rassf5 SARAH domain and a 1:1 heterodimer formation. The linker, region between the kinase and the SARAH domain is shown to be disordered, in the free protein. These results imply a novel mode of interaction with, RASSF family proteins and provide insight into the mechanism of apoptosis, control by the SARAH domain.
About this Structure
2JO8 is a Single protein structure of sequence from Homo sapiens. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
Structural insight into dimeric interaction of the SARAH domains from Mst1 and RASSF family proteins in the apoptosis pathway., Hwang E, Ryu KS, Paakkonen K, Guntert P, Cheong HK, Lim DS, Lee JO, Jeon YH, Cheong C, Proc Natl Acad Sci U S A. 2007 May 29;104(22):9236-41. Epub 2007 May 21. PMID:17517604
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