2J8O

Structure of the immunoglobulin tandem repeat of titin A168-A169

Summary for 2J8O

• Entry DOI: 10.2210/pdb2j8o/pdb
• Related: 1BPV 1G1C 1NCT 1NCU 1TIT 1TIU 1TKI 1TNM 1TNN 1WAA 1YA5 2A38 2BK8 2F8V 2J8H
• Descriptor: TITIN, GLYCEROL (3 entities in total)
• Functional Keywords: cardiomyopathy, nuclear protein, serine/threonine-protein kinase, limb-girdle muscular dystrophy, phosphorylation, disease mutation, structural protein, titin, a-band, kinase, wd repeat, tpr repeat, immunoglobulin domain, immunoglobulin like domain, nucleotide-binding, atp-binding, transferase, kelch repeat
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 2
• Total formula weight: 43715.83

Authors

Mueller, S.,Lange, S.,Kursula, I.,Gautel, M.,Wilmanns, M. (deposition date: 2006-10-26, release date: 2007-08-21, Last modification date: 2023-12-13)

Primary citation

Mueller, S.,Lange, S.,Gautel, M.,Wilmanns, M.
Rigid Conformation of an Immunoglobulin Domain Tandem Repeat in the A-Band of the Elastic Muscle Protein Titin
J.Mol.Biol., 371:469-, 2007

PubMed Abstract: Most of the structure of the giant muscle protein titin is formed by small modular domains. Many of them are predicted to be arranged in repeats with short linkers that may be key determinants of the peculiar elastic properties of titin. Here, we present the molecular structure of a tandem arrangement of two immunoglobulin-like domains, A168 and A169, located within the A-band segment of titin. The two domains are connected by a 17 residue long beta-strand and form a common interface. Based on these data, we establish general principles to estimate the amount of conformational flexibility of tandem domain motifs in titin. An unusual bulge within the second domain, A169, is directly involved into binding to a sarcomeric ligand, MURF-1, thus suggesting a dual role of this tandem for both the mechanical properties of titin and for sarcomeric signaling.

PubMed: 17574571
DOI: 10.1016/J.JMB.2007.05.055

Experimental method

X-RAY DIFFRACTION (2.49 Å)