Structure of mouse muskelin discoidin domain and biochemical characterization of its self-association
- Authors
- Kim, Kook-Han; Hong, Seung Kon; Hwang, Kwang Yeon; Kim, Eunice EunKyeong
- Issue Date
- 11월-2014
- Publisher
- INT UNION CRYSTALLOGRAPHY
- Keywords
- CTLH complex; discoidin domain; kelch repeat; muskelin; self-association
- Citation
- ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, v.70, pp.2863 - 2874
- Indexed
- SCIE
SCOPUS
- Journal Title
- ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
- Volume
- 70
- Start Page
- 2863
- End Page
- 2874
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/96887
- DOI
- 10.1107/S139900471401894X
- ISSN
- 2059-7983
- Abstract
- 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.
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