Obscurin: Difference between revisions
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'''Obscurin''' (Obs) is a giant sarcomeric signalling protein expressed in striated muscles. Other giant proteins in the family include titin and nebulin. It is a multidomain protein containing adhesion modules and signaling domains. These domains include: 68 Ig domains, 2 fibronectin domains, 1 calcium/calmodulin-binding domain, 1 RhoGEF domain with PH domain and 2 serine/thereonine kinase domains. | '''Obscurin''' (Obs) is a giant sarcomeric signalling protein expressed in striated muscles. Other giant proteins in the family include titin and nebulin. It is a multidomain protein containing adhesion modules and signaling domains. These domains include: 68 Ig domains, 2 fibronectin domains, 1 calcium/calmodulin-binding domain, 1 RhoGEF domain with PH domain and 2 serine/thereonine kinase domains. | ||
Obscurin binds small ankyrin 1 which is part of the sarcoplasmic reticulum membrane. It associates with the contractile apparatus via binding to titin and sarcomeric myosin. Obscurin is assumed to play a key role in modulating the organization and assembly of sarcomeric reticulum and the myofibril. | Obscurin binds small ankyrin 1 which is part of the sarcoplasmic reticulum membrane. It associates with the contractile apparatus via binding to titin and sarcomeric myosin. Obscurin is assumed to play a key role in modulating the organization and assembly of sarcomeric reticulum and the myofibril. For more details see [[Group:MUZIC:Obscurin]]. | ||
==3D structures of obscurin== | ==3D structures of obscurin== | ||
