PDBsum entry 4pqq

Protein binding

PDB id

4pqq

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Contents

			Protein chain

					156 a.a.

			Ligands

					PO4


					PG4 ×2

			Waters ×203

PDB id:

4pqq

Links

Name:

Protein binding

Title:

The crystal structure of discoidin domain from muskelin

Structure:

Muskelin. Chain: a. Fragment: n-terminal domain, unp residues 12-167. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: mkln1. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.55Å

R-factor:

0.155

R-free:

0.176

Authors:

K.-H.Kim,S.K.Hong,E.E.Kim

Key ref:

K.H.Kim et al. (2014). Structure of mouse muskelin discoidin domain and biochemical characterization of its self-association. Acta Crystallogr D Biol Crystallogr, 70, 2863-2874. PubMed id: 25372678 DOI: 10.1107/S139900471401894X

Date:

04-Mar-14

Release date:

12-Nov-14

PROCHECK

	Headers

	References

Protein chain

O89050 (MKLN1_MOUSE) - Muskelin from Mus musculus

Seq: Struc:

Seq: Struc:					735 a.a. 156 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

DOI no: 10.1107/S139900471401894X	Acta Crystallogr D Biol Crystallogr 70:2863-2874 (2014)
PubMed id: 25372678

Structure of mouse muskelin discoidin domain and biochemical characterization of its self-association.
K.H.Kim, S.K.Hong, K.Y.Hwang, E.E.Kim.

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.