Kim, Kook-Han Hong, Seung Kon Hwang, Kwang Yeon Kim, Eunice EunKyeong 2024-01-20T08:32:56Z 2024-01-20T08:32:56Z 2021-09-02 2014-11 2059-7983 https://pubs.kist.re.kr/handle/201004/126189 Muskelin is an intracellular kelch-repeat protein comprised of discoidin, LisH, CTLH and kelch-repeat domains. It is involved in cell adhesion and the regulation of cytoskeleton dynamics as well as being a component of a putative E3 ligase complex. Here, the first crystal structure of mouse muskelin discoidin domain (MK-DD) is reported at 1.55 angstrom resolution, which reveals a distorted eight-stranded beta-barrel with two short alpha-helices at one end of the barrel. Interestingly, the Nand C-termini are not linked by the disulfide bonds found in other eukaryotic discoidin structures. A highly conserved MIND motif appears to be the determinant for MK-DD specific interaction together with the spike loops. Analysis of interdomain interaction shows that MK-DD binds the kelch-repeat domain directly and that this interaction depends on the presence of the LisH domain. English INT UNION CRYSTALLOGRAPHY LACTADHERIN C2 DOMAIN CRYSTAL-STRUCTURE GALACTOSE-OXIDASE BINDING PROTEIN RECEPTOR RECOGNITION EXPRESSION MEDIATOR SUBUNIT Structure of mouse muskelin discoidin domain and biochemical characterization of its self-association Article 10.1107/S139900471401894X 1 Acta Crystallographica Section D - Structural Biology, v.70, pp.2863 - 2874 Acta Crystallographica Section D - Structural Biology 70 2863 2874 scie scopus 000344792000009 2-s2.0-84908622925 Biochemical Research Methods Biochemistry & Molecular Biology Biophysics Crystallography Biochemistry & Molecular Biology Biophysics Crystallography Article LACTADHERIN C2 DOMAIN CRYSTAL-STRUCTURE GALACTOSE-OXIDASE BINDING PROTEIN RECEPTOR RECOGNITION EXPRESSION MEDIATOR SUBUNIT CTLH complex discoidin domain kelch repeat muskelin self-association