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Sequence motifs of myelin membrane proteins: Towards the molecular basis of diseases.
MedLine Citation:
PMID:  23339078     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The shortest sequence of amino acids in protein containing functional and structural information is a "motif." To understand myelin protein functions, we intensively searched for motifs that can be found in myelin proteins. Some myelin proteins had several different motifs or repetition of the same motif. The most abundant motif found among myelin proteins was a myristoylation motif. Bovine MAG held 11 myristoylation motifs and human myelin basic protein held as many as eight such motifs. PMP22 had the fewest myristoylation motifs, which was only one; rat PMP22 contained no such motifs. Cholesterol recognition/interaction amino-acid consensus (CRAC) motif was not found in myelin basic protein. P2 protein of different species contained only one CRAC motif, except for P2 of horse, which had no such motifs. MAG, MOG, and P0 were very rich in CRAC, three to eight motifs per protein. The analysis of motifs in myelin proteins is expected to provide structural insight and refinement of predicted 3D models for which structures are as yet unknown. Analysis of motifs in mutant proteins associated with neurological diseases uncovered that some motifs disappeared in P0 with mutation found in neurological diseases. There are 2,500 motifs deposited in a databank, but 21 were found in myelin proteins, which is only 1% of the total known motifs. There was great variability in the number of motifs among proteins from different species. The appearance or disappearance of protein motifs after gaining point mutation in the protein related to neurological diseases was very interesting. © 2013 Wiley Periodicals, Inc.
Authors:
Jan Sedzik; Jan Pawel Jastrzebski; Kazuhiro Ikenaka
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-22
Journal Detail:
Title:  Journal of neuroscience research     Volume:  -     ISSN:  1097-4547     ISO Abbreviation:  J. Neurosci. Res.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-22     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7600111     Medline TA:  J Neurosci Res     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2013 Wiley Periodicals, Inc.
Affiliation:
Department of Chemical Engineering, Protein Crystallization Facility, Royal Institute of Technology, Stockholm, Sweden; Department of Neuroscience and Bioinformatics, National Institute of Physiological Sciences, Okazaki, Japan; Department of Applied Chemistry, School of Engineering, The University of Tokyo, Tokyo, Japan. sedzik@kth.se.
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