MP-T: improving membrane protein alignment for structure prediction
Author(s) -
Jamie Hill,
Charlotte M. Deane
Publication year - 2012
Publication title -
bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.599
H-Index - 390
eISSN - 1367-4811
pISSN - 1367-4803
DOI - 10.1093/bioinformatics/bts640
Subject(s) - multiple sequence alignment , structural alignment , sequence alignment , membrane protein , sequence (biology) , computational biology , alignment free sequence analysis , peptide sequence , membrane , protein structure , computer science , protein secondary structure , bioinformatics , biology , biochemistry , gene
Membrane proteins are clinically relevant, yet their crystal structures are rare. Models of membrane proteins are typically built from template structures with low sequence identity to the target sequence, using a sequence-structure alignment as a blueprint. This alignment is usually made with programs designed for use on soluble proteins. Biological membranes have layers of varying hydrophobicity, and membrane proteins have different amino-acid substitution preferences from their soluble counterparts. Here we include these factors into an alignment method to improve alignments and consequently improve membrane protein models.
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