PDBsum entry 2kdg

Structural protein

PDB id: 2kdg

Contents

Protein chain

100 a.a. *

* Residue conservation analysis

PDB id:

2kdg

Name:

Structural protein

Title:

Solution structure of the 1st ig domain of myotilin

Structure:

Myotilin. Chain: a. Fragment: the first immunoglobulin domain (residues 249-344). Synonym: titin immunoglobulin domain protein, myofibrillar titin-like ig domains protein, 57 kda cytoskeletal protein. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: myot, ttid. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

25 models

Authors:

O.Heikkinen,I.Kilpelainen,P.Permi,H.Koskela,J.Ylanne,O.Carpen

Key ref:

O.Heikkinen et al. (2009). Solution structure of the first immunoglobulin domain of human myotilin. J Biomol Nmr, 44, 107-112. PubMed id: 19418025

Date:

08-Jan-09 Release date: 21-Jul-09

Protein chain

Q9UBF9  (MYOTI_HUMAN) -  Myotilin from Homo sapiens

Seq: 498 a.a.

Struc: 100 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

J Biomol Nmr 44:107-112 (2009)

PubMed id: 19418025

Solution structure of the first immunoglobulin domain of human myotilin.

O.Heikkinen, P.Permi, H.Koskela, O.Carpén, J.Ylänne, I.Kilpeläinen.

ABSTRACT

Myotilin is a 57 kDa actin-binding and -bundling protein that consists of a unique serine-rich amino-terminus, two Ig-domains and a short carboxy-terminus with a PDZ-binding motif. Myotilin localizes in sarcomeric Z-discs, where it interacts with several sarcomeric proteins. Point mutations in myotilin cause muscle disorders morphologically highlighted by sarcomeric disarray and aggregation. The actin-binding and dimerization propensity of myotilin has been mapped to the Ig-domains. Here we present high-resolution structure of the first Ig-domain of myotilin (MyoIg1) determined with solution state NMR spectroscopy. Nearly complete chemical shift assignments of MyoIg1 were achieved despite several missing backbone 1H-15N-HSQC signals. The structure derived from distance and dihedral angle restraints using torsion angle dynamics was further refined using molecular dynamics. The structure of MyoIg1 exhibits I-type Ig-fold. The absence of several backbone 1H-15N-HSQC signals can be explained by conformational exchange taking place at the hydrophobic core of the protein.