4pqq

Publication Abstract from PubMed

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 A resolution, which reveals a distorted eight-stranded beta-barrel with two short alpha-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.

Structure of mouse muskelin discoidin domain and biochemical characterization of its self-association.,Kim KH, Hong SK, Hwang KY, Kim EE Acta Crystallogr D Biol Crystallogr. 2014 Nov;70(Pt 11):2863-74. doi:, 10.1107/S139900471401894X. Epub 2014 Oct 16. PMID:25372678^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.