title: PoreLogo: a new tool to analyse, visualize and compare channels in transmembrane proteins.
abstract: The increasing number of available atomic 3D structures of transmembrane channel proteins represents a valuable resource for better understanding their structure-function relationships and to eventually predict their selectivity. Herein, we present PoreLogo, an automatic tool for analysing, visualizing and comparing the amino acid composition of transmembrane channels and its conservation across the corresponding protein family.
  
  
  BACKGROUND
  PoreLogo is accessible as a public web server at http://www.ebi.ac.uk/thornton-srv/software/PoreLogo/.
authors.affiliation: Department of Applied Sciences, University of Parthenope of Naples, Centro Direzionale Isola C4 80143, Naples, Italy. romina.oliva@uniparthenope.it
authors.forename: Romina
authors.initials: R
authors.lastname: Oliva
authors.forename: Janet M
authors.initials: JM
authors.lastname: Thornton
authors.forename: Marialuisa
authors.initials: M
authors.lastname: Pellegrini-Calace
mesh_terms: D000595:Amino Acid Sequence; D019295:Computational Biology / Q000379:methods*; D030562:Databases, Protein; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D020539:Sequence Analysis, Protein / Q000379:methods*; D012984:Software
chemical_list: D008565:Membrane Proteins