Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2011-2-28
pubmed:abstractText
Activin receptor type IIB (ActRIIB) belongs to a type II transforming growth factor-? (TGF-?) serine/threonine kinase receptor family which is integral to the activin and myostatin signaling pathway. Actvin and myostatin bind to activin type II receptors (ActRIIA and ActRIIB), and the glycine-serine-rich domains of type I receptors are phosphorylated by type II receptors. Activin enhances follicle-stimulating hormone biosynthesis and secretion and is involved in apoptosis, fibrosis, inflammation, and neurogenesis. Because of its essential role, activin is regarded as a novel drug target. Myostatin, also referred as growth and differentiation factor 8 (GDF-8), modulates skeletal muscle growth and has been a therapeutic target for disease conditions such as muscular dystrophy, sarcopenia, cashexia, and diabetes mellitus. The AcRIIB kinase domain from human represents a distinct type II receptor serine/threonine kinase subfamily identifiable in part by common features of Thr265 as a gatekeeper residue and back pocket supported by Phe247. The human ActRII kinase domain structure provides a basis for a more integrated understanding of substrate recognition and catalysis and will also be of help for developing chemical inhibitors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0083-6729
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 Elsevier Inc. All rights reserved.
pubmed:issnType
Print
pubmed:volume
85
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
29-38
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Crystal structure of activin receptor type IIB kinase domain.
pubmed:affiliation
Pfizer Inc., Pfizer Global Research & Development, Groton, Connecticut, USA.
pubmed:publicationType
Journal Article, Review