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 Å resolution, which reveals a distorted eight-stranded β-barrel with two short α-helices at one end of the barrel. Interestingly, the N- and 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.
Original language | English |
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Pages (from-to) | 2863-2874 |
Number of pages | 12 |
Journal | Acta Crystallographica Section D: Biological Crystallography |
Volume | 70 |
Issue number | 11 |
DOIs | |
Publication status | Published - 2014 Nov 1 |
Keywords
- CTLH complex
- discoidin domain
- kelch repeat
- muskelin
- self-association
ASJC Scopus subject areas
- Structural Biology