3KNB

Crystal structure of the titin C-terminus in complex with obscurin-like 1

Replaces:  3IRG

Summary for 3KNB

• Entry DOI: 10.2210/pdb3knb/pdb
• Descriptor: Titin, Obscurin-like protein 1, SULFATE ION, ... (4 entities in total)
• Functional Keywords: ig-like, titin, obscurin, obsl1, atp-binding, calmodulin-binding, cardiomyopathy, disease mutation, immunoglobulin domain, kinase, limb-girdle muscular dystrophy, magnesium, nucleotide-binding, nucleus, phosphoprotein, serine/threonine-protein kinase, transferase, structural protein-structural protein complex, structural protein/structural protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm : Q8WZ42 O75147
• Total number of polymer chains: 2
• Total formula weight: 21820.56

Authors

Sauer, F.,Vahokoski, J.,Wilmanns, M. (deposition date: 2009-11-12, release date: 2009-12-01, Last modification date: 2024-02-21)

Primary citation

Sauer, F.,Vahokoski, J.,Song, Y.H.,Wilmanns, M.
Molecular basis of the head-to-tail assembly of giant muscle proteins obscurin-like 1 and titin.
Embo Rep., 11:534-540, 2010

PubMed Abstract: Large filament proteins in muscle sarcomeres comprise many immunoglobulin-like domains that provide a molecular platform for self-assembly and interactions with heterologous protein partners. We have unravelled the molecular basis for the head-to-tail interaction of the carboxyl terminus of titin and the amino-terminus of obscurin-like-1 by X-ray crystallography. The binary complex is formed by a parallel intermolecular beta-sheet that presents a novel immunoglobulin-like domain-mediated assembly mechanism in muscle filament proteins. Complementary binding data show that the assembly is entropy-driven rather than dominated data by specific polar interactions. The assembly observed leads to a V-shaped zipper-like arrangement of the two filament proteins.

PubMed: 20489725
DOI: 10.1038/embor.2010.65

Experimental method

X-RAY DIFFRACTION (1.4 Å)