2KDG

Solution Structure of the 1st Ig domain of Myotilin

Summary for 2KDG

• Entry DOI: 10.2210/pdb2kdg/pdb
• Descriptor: Myotilin (1 entity in total)
• Functional Keywords: myotilin, immonoglobulin domain, actin-binding, structural protein, cell membrane, cytoplasm, cytoskeleton, disease mutation, immunoglobulin domain, limb-girdle muscular dystrophy, membrane, muscle protein, polymorphism
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane, sarcolemma: Q9UBF9
• Total number of polymer chains: 1
• Total formula weight: 10971.52

Authors

Heikkinen, O.,Kilpelainen, I.,Permi, P.,Koskela, H.,Ylanne, J.,Carpen, O. (deposition date: 2009-01-08, release date: 2009-07-21, Last modification date: 2024-05-29)

Primary citation

Heikkinen, O.,Permi, P.,Koskela, H.,Carpen, O.,Ylanne, J.,Kilpelainen, I.
Solution structure of the first immunoglobulin domain of human myotilin
J.Biomol.Nmr, 44:107-112, 2009

PubMed 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.

PubMed: 19418025
DOI: 10.1007/s10858-009-9320-4

Experimental method

SOLUTION NMR