An adhesion molecule involved in muscular dystrophies: structural and functional analysis of dystroglycan domains.
Dystroglycan (DG) plays a pivotal role within the dystrophin-glycoprotein complex (DGC) which represents a major factor for muscle fibre stability upon contraction. It has been shown that many muscular dystrophy phenotypes are caused by mutations of proteins belonging to or being associated with the DGC. Due to its prominent role for muscle stability, the detailed knowledge of DG structural and functional aspects should be considered of primary importance in order to develop new treatments for neuromuscular diseases.
Brancaccio
Andrea
A
CNR, Istituto di Chimica del Riconoscimento Molecolare, Istituto di Biochimica e Biochimica Clinica, Universita' Cattolica del Sacro Cuore, 00168 Rome, Italy. a.brancaccio@uniserv.ccr.rm.cnr.it
D000818:Animals; D003593:Cytoplasm / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000737:chemistry* / Q000502:physiology*; D049030:Dystroglycans; D005109:Extracellular Matrix / Q000378:metabolism; D006801:Humans; D008562:Membrane Glycoproteins / Q000737:chemistry* / Q000502:physiology*; D008954:Models, Biological; D009136:Muscular Dystrophies; D009154:Mutation; D010641:Phenotype; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship
D003598:Cytoskeletal Proteins; C483081:DAG1 protein, human; D008562:Membrane Glycoproteins; D049030:Dystroglycans