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Structural Properties of the Myelin‐Associated Glycoprotein Ectodomain
Author(s) -
Attia John,
Hicks Les,
Oikawa Kimio,
Kay Cyril M.,
Dunn Robert J.
Publication year - 1993
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1993.tb02178.x
Subject(s) - ectodomain , glycoprotein , myelin associated glycoprotein , myelin , biophysics , chemistry , extracellular , divalent , molecule , dimer , crystallography , biochemistry , biology , receptor , neuroscience , central nervous system , organic chemistry
Myelin‐associated glycoprotein (MAG) has been proposed to mediate adhesive interactions during myelin development. We have used the baculovirus expression system to produce a truncated form of this molecule [soluble extracellular domain of MAG (sMAG)] consisting of the complete extracellular ectodomain. Spectroscopic studies indicate a high β‐sheet content, consistent with the prediction of Ig‐like structure. Hydrodynamic studies indicate an asymmetric monomer, with a Stokes radius of 4.1–4.6 nm, a sedimentation coefficient of 3.6S, and a frictional ratio of ∼1.6. We postulate that the outer two Ig‐like domains form a unit that folds back over the rest of the molecule. Fluorescence quenching studies indicate that sMAG interacts with divalent cations and may have a functional lectin domain.