4PQQ

The crystal structure of discoidin domain from muskelin

Summary for 4PQQ

• Entry DOI: 10.2210/pdb4pqq/pdb
• Descriptor: Muskelin, PHOSPHATE ION, TETRAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: jelly-roll, cell spreading mediator, prostaglandin ep3 receptor, alpha isoform, ranbp9, phosphorylation, protein binding
• Biological source: Mus musculus (mouse)
• Cellular location: Cytoplasm: O89050
• Total number of polymer chains: 1
• Total formula weight: 18764.34

Authors

Kim, K.-H.,Hong, S.K.,Kim, E.E. (deposition date: 2014-03-04, release date: 2014-11-12, Last modification date: 2024-02-28)

Primary citation

Kim, K.H.,Hong, S.K.,Hwang, K.Y.,Kim, E.E.
Structure of mouse muskelin discoidin domain and biochemical characterization of its self-association.
Acta Crystallogr.,Sect.D, 70:2863-2874, 2014

PubMed 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.

PubMed: 25372678
DOI: 10.1107/S139900471401894X

Experimental method

X-RAY DIFFRACTION (1.55 Å)