Biomaterial Database

Titin and nebulin: protein rulers in muscle? 1994

J Trinick

Division of Molecular and Cellular Biology, Bristol University School of Veterinary Science, Langford, UK.

Titin and nebulin are giant muscle proteins, both of which are approximately 1 micron long and are composed of many repeating domains. Titin domains resemble type III fibronectin and C-2 immunoglobulins. Both proteins are likely to be involved in specifying and stabilizing the highly ordered structure of muscle, probably by acting as 'protein rulers' to regulate the assembly of myosin and actin filaments precisely.

UI	MeSH Term	Description	Entries
D008958	Models, Molecular	Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.	Molecular Models,Model, Molecular,Molecular Model
D009124	Muscle Proteins	The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN.	Muscle Protein,Protein, Muscle,Proteins, Muscle
D009132	Muscles	Contractile tissue that produces movement in animals.	Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D010766	Phosphorylation	The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.	Phosphorylations
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D011494	Protein Kinases	A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.	Protein Kinase,Kinase, Protein,Kinases, Protein
D004548	Elasticity	Resistance and recovery from distortion of shape.
D000199	Actins	Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.	F-Actin,G-Actin,Actin,Isoactin,N-Actin,alpha-Actin,alpha-Isoactin,beta-Actin,gamma-Actin,F Actin,G Actin,N Actin,alpha Actin,alpha Isoactin,beta Actin,gamma Actin
D064211	Connectin	A giant elastic protein of molecular mass ranging from 2,993 kDa (cardiac), 3,300 kDa (psoas), to 3,700 kDa (soleus) having a kinase domain. The amino- terminal is involved in a Z line binding, and the carboxy-terminal region is bound to the myosin filament with an overlap between the counter-connectin filaments at the M line.	M-Band Proteins,M-Line 185 kDa Protein,M-Protein (muscle),Muscle M-Line Protein,Myomesin,Skelemins,Titin,Titin 1,Titin 2,Titin Kinase,alpha-Connectin,beta-Connectin,Kinase, Titin,M Band Proteins,M Line 185 kDa Protein,M-Line Protein, Muscle,Muscle M Line Protein,Protein, Muscle M-Line,Proteins, M-Band,alpha Connectin,beta Connectin