Abstract:
:Myelin basic protein (MBP) is predominantly found in the membranes of the myelin sheath of the central nervous system and is involved in important protein-protein and protein-lipid interactions in vivo and in vitro. Furthermore, divalent transition metal ions, especially Zn(2+) and Cu(2+), seem to directly affect the MBP-mediated formation and stabilization of the myelin sheath of the central nervous system. MBP belongs to the realm of intrinsically disordered proteins, and only fragmentary information is available regarding its partial structure(s) or supramolecular arrangements. Here, using standard continuous wave and modern pulse electron paramagnetic resonance methods, as well as dynamic light scattering, we demonstrate the uptake and specific coordination of two Cu(2+) atoms or one Zn(2+) atom per MBP molecule in solution. In the presence of phosphates, further addition of divalent metal ions above a characteristic threshold of four Cu(2+) atoms or two Zn(2+) atoms per MBP molecule leads to the formation of large MBP aggregates within the protein solution. In vivo, MBP-MBP interactions may thus be mediated by divalent cations.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Bund T,Boggs JM,Harauz G,Hellmann N,Hinderberger Ddoi
10.1016/j.bpj.2010.08.022subject
Has Abstractpub_date
2010-11-03 00:00:00pages
3020-8issue
9eissn
0006-3495issn
1542-0086pii
S0006-3495(10)00991-4journal_volume
99pub_type
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