Animals; Binding Sites; Calcium/chemistry/metabolism; Calmodulin/chemistry/genetics/metabolism; Mice; Myelin Basic Protein/chemistry/genetics/metabolism; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary
Abstract :
[en] Myelin basic protein (MBP), specifically the 18.5 kDa isoform, is a peripheral membrane protein and a major component of mammalian central nervous system myelin. It is an intrinsically disordered and multifunctional protein that binds cytoskeletal and other cytosolic proteins to a membrane surface and thereby acquires ordered structure. These associations are modulated by post-translational modifications of MBP, as well as by interactions of MBP with Ca(2+)-calmodulin (CaM). Enzymatic deimination of usually six arginine residues to citrulline results in a decrease in the net positive charge of the protein from 19 to
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Homchaudhuri, Lopamudra
De Avila, Miguel
Nilsson, Stina B.
Bessonov, Kyrylo ; Université de Liège - ULiège > Dép. d'électric., électron. et informat. (Inst.Montefiore) > Bioinformatique
Smith, Graham S. T.
Bamm, Vladimir V.
Musse, Abdiwahab A.
Harauz, George
Boggs, Joan M.
Language :
English
Title :
Secondary structure and solvent accessibility of a calmodulin-binding C-terminal segment of membrane-associated myelin basic protein.
Publication date :
2010
Journal title :
Biochemistry
ISSN :
0006-2960
eISSN :
1520-4995
Publisher :
American Chemical Society (ACS), Washington, United States - District of Columbia
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