2j8h
From Proteopedia
| Line 6: | Line 6: | ||
==Overview== | ==Overview== | ||
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. | 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. | ||
| + | |||
| + | ==Disease== | ||
| + | Known diseases associated with this structure: Cardiomyopathy, dilated, 1G OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188840 188840]], Cardiomyopathy, familial hypertrophic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188840 188840]], Muscular dystrophy, limb-girdle, type 2J OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188840 188840]], Myopathy, proximal, with early respiratory muscle involvement OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188840 188840]], Tibial muscular dystrophy, tardive OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188840 188840]] | ||
==About this Structure== | ==About this Structure== | ||
| Line 43: | Line 46: | ||
[[Category: wd repeat]] | [[Category: wd repeat]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:52:53 2007'' |
Revision as of 20:46, 12 November 2007
|
STRUCTURE OF THE IMMUNOGLOBULIN TANDEM REPEAT A168-A169 OF TITIN
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Cardiomyopathy, dilated, 1G OMIM:[188840], Cardiomyopathy, familial hypertrophic OMIM:[188840], Muscular dystrophy, limb-girdle, type 2J OMIM:[188840], Myopathy, proximal, with early respiratory muscle involvement OMIM:[188840], Tibial muscular dystrophy, tardive OMIM:[188840]
About this Structure
2J8H is a Single protein structure of sequence from Homo sapiens with GOL as ligand. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Rigid Conformation of an Immunoglobulin Domain Tandem Repeat in the A-band of the Elastic Muscle Protein Titin., Muller S, Lange S, Gautel M, Wilmanns M, J Mol Biol. 2007 Aug 10;371(2):469-80. Epub 2007 May 25. PMID:17574571
Page seeded by OCA on Mon Nov 12 22:52:53 2007
Categories: Homo sapiens | Non-specific serine/threonine protein kinase | Single protein | Gautel, M. | Kursula, I. | Lange, S. | Mueller, S. | Wilmanns, M. | GOL | A-band | Alternative splicing | Atp-binding | Cardiomyopathy | Coiled coil | Disease mutation | Immunoglobulin domain | Immunoglobulin like domain | Kelch repeat | Kinase | Limb-girdle muscular dystrophy | Nuclear protein | Nucleotide-binding | Phosphorylation | Polymorphism | Serine/threonine-protein kinase | Structural protein | Titin | Tpr repeat | Transferase | Wd repeat
