1G1C

I1 DOMAIN FROM TITIN

Summary for 1G1C

• Entry DOI: 10.2210/pdb1g1c/pdb
• Descriptor: IMMUNOGLOBULIN-LIKE DOMAIN I1 FROM TITIN (2 entities in total)
• Functional Keywords: immunoglobulin domain, beta-sandwhich, i-set, structural protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 22479.36

Authors

Mayans, O.,Wuerges, J.,Gautel, M.,Wilmanns, M. (deposition date: 2000-10-11, release date: 2001-10-12, Last modification date: 2024-10-30)

Primary citation

Mayans, O.,Wuerges, J.,Canela, S.,Gautel, M.,Wilmanns, M.
Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin.
Structure, 9:331-340, 2001

PubMed Abstract: The giant muscle protein titin contributes to the filament system in skeletal and cardiac muscle cells by connecting the Z disk and the central M line of the sarcomere. One of the physiological functions of titin is to act as a passive spring in the sarcomere, which is achieved by the elastic properties of its central I band region. Titin contains about 300 domains of which more than half are folded as immunoglobulin-like (Ig) domains. Ig domain segments of the I band of titin have been extensively used as templates to investigate the molecular basis of protein elasticity.

PubMed: 11525170
DOI: 10.1016/s0969-2126(01)00591-3

Experimental method

X-RAY DIFFRACTION (2.1 Å)