Molecular dynamics exposes α-helices in myelin basic protein

被引：18

作者：

Bates, IR

Harauz, G

机构：

[1] Univ Guelph, Dept Mol Biol & Genet, Guelph, ON N1G 2W1, Canada

[2] Univ Guelph, Biophys Interdepartmental Grp, Guelph, ON N1G 2W1, Canada

来源：

JOURNAL OF MOLECULAR MODELING | 2003年 / 9卷 / 05期

关键词：

myelin basic protein (MBP); mutagenesis; deimination; citrulline; molecular dynamics; electrostatic potentials; protein structure;

D O I：

10.1007/s00894-003-0145-x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Molecular dynamics simulations of models of unmodified and deiminated MBP (myelin basic protein) have been performed on solvated structures with added counterions, for 10 ns using AMBER (assisted model building with energy refinement). The protein structures became extended, and a considerable number of alpha-helical segments formed spontaneously. The degree of molecular extension was greater in the deiminated species, and the alpha-helices were more transient. These structural disruptions may be operative in vivo during multiple sclerosis.

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收藏

页码：290 / 297

页数：8

相关论文

共 80 条

[1]

*ACC INC, 2000, INSIGHT2000 DS VIEW

[2] FORCES BETWEEN PROTEINS AND MODEL POLYPEPTIDES ADSORBED ON MICA SURFACES [J].

AFSHARRAD, T ;

BAILEY, AI ;

LUCKHAM, PF ;

MACNAUGHTAN, W ;

CHAPMAN, D .

BIOCHIMICA ET BIOPHYSICA ACTA, 1987, 915 (01) :101-111

[3] Effect of phosphorylation on α-helix stability as a function of position [J].

Andrew, CD ;

Warwicker, J ;

Jones, GR ;

Doig, AJ .

BIOCHEMISTRY, 2002, 41 (06) :1897-1905

[4] Membrane-anchoring and charge effects in the interaction of myelin basic protein with lipid bilayers studied by site-directed spin labeling [J].

Bates, IR ;

Boggs, JM ;

Feix, JB ;

Harauz, G .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (31) :29041-29047

[5] An Arg/Lys→Gln mutant of recombinant murine myelin basic protein as a mimic of the deiminated form implicated in multiple sclerosis [J].

Bates, IR ;

Libich, DS ;

Wood, DD ;

Moscarello, MA ;

Harauz, G .

PROTEIN EXPRESSION AND PURIFICATION, 2002, 25 (02) :330-341

[6] Characterization of a recombinant murine 18.5-kDa myelin basic protein [J].

Bates, IR ;

Matharu, P ;

Ishiyama, N ;

Rochon, D ;

Wood, DD ;

Polverini, E ;

Moscarello, MA ;

Viner, NJ ;

Harauz, G .

PROTEIN EXPRESSION AND PURIFICATION, 2000, 20 (02) :285-299

[7] Three-dimensional structure of myelin basic protein .1. Reconstruction via angular reconstitution of randomly oriented single particles [J].

Beniac, DR ;

Luckevich, MD ;

Czarnota, GJ ;

Tompkins, TA ;

Ridsdale, RA ;

Ottensmeyer, FP ;

Moscarello, MA ;

Harauz, G .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (07) :4261-4268

[8] Cryoelectron microscopy of protein-lipid complexes of human myelin basic protein charge isomers differing in degree of citrullination [J].

Beniac, DR ;

Wood, DD ;

Palaniyar, N ;

Ottensmeyer, FP ;

Moscarello, MA ;

Harauz, G .

JOURNAL OF STRUCTURAL BIOLOGY, 2000, 129 (01) :80-95

[9] The Protein Data Bank [J].

Berman, HM ;

Battistuz, T ;

Bhat, TN ;

Bluhm, WF ;

Bourne, PE ;

Burkhardt, K ;

Iype, L ;

Jain, S ;

Fagan, P ;

Marvin, J ;

Padilla, D ;

Ravichandran, V ;

Schneider, B ;

Thanki, N ;

Weissig, H ;

Westbrook, JD ;

Zardecki, C .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2002, 58 :899-907

[10]

Boggs JM, 1999, J NEUROSCI RES, V57, P529, DOI 10.1002/(SICI)1097-4547(19990815)57:4<529::AID-JNR12>3.0.CO

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