Substitutions mimicking deimination and phosphorylation of 18.5-kDa myelin basic protein exert local structural effects that subtly influence its global folding
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- 作者：Kenrick A. Vassalla ; 1 ; Vladimir V. Bamma ; 1 ; Andrew D. Jenkinsa ; 2 ; Caroline J. Veltea ; b ; 3 ; Daniel R. Kattnigb ; 4 ; Joan M. Boggsc ; d ; Dariush Hinderbergerb ; 5 ; George Harauza ; gharauz@uoguelph.ca" class="auth_mail" title="E-mail the corresponding author
- 关键词：ANS ; anilinonaphthalene-1-sulfonic acid ; C1 ; least-modified charge component of 18.5-kDa MBP ; C8 ; most-modified charge component of 18.5-kDa MBP (usually highly-deiminated) ; Ca2 ; +-CaM ; calcium-activated calmodulin ; CatD ; cathepsin D ; CD ; circular dichroism ; Cyt-LUV ; cytoplasmic LUV ; DEER ; double-electron&ndash ; electron resonance ; EPR ; electron paramagnetic resonance ; FRET ; Fö ; rster (fluorescence) resonance energy transfer ; IAEDANS ; 5-((((2-iodoacetyl) amino) ethyl) amino) naphthalene-1-
- 刊名：Biochimica et Biophysica Acta (BBA)-Biomembranes
- 出版年：2016
- 出版时间：June 2016
- 年：2016
- 卷：1858
- 期：6
- 页码：1262-1277
- 全文大小：2288 K
文摘
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Myelin basic protein (MBP) is a multifunctional intrinsically-disordered protein.
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MBP populates three energetically distinct and reversible equilibrium conformations.
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MBP's equilibrium conformational states are chimeras of globule and coil structures.
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Charge reduction (deimination) shifts distribution but not lateral packing density.
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Charge reduction (deimination) favors compaction of expanded conformational states.
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Threonyl phosphorylation has only local conformational effects.