ARCHITECTURE OF BETA-BARREL MEMBRANE-PROTEINS - ANALYSIS OF TRIMERIC PORINS

Citation
K. Seshadri et al., ARCHITECTURE OF BETA-BARREL MEMBRANE-PROTEINS - ANALYSIS OF TRIMERIC PORINS, Protein science, 7(9), 1998, pp. 2026-2032
Citations number
27
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biology
Journal title
ISSN journal
0961-8368
Volume
7
Issue
9
Year of publication
1998
Pages
2026 - 2032
Database
ISI
SICI code
0961-8368(1998)7:9<2026:AOBM-A>2.0.ZU;2-R
Abstract
We have analyzed the known three-dimensional structures of trimeric po rins from bacterial outer membranes. The distribution of surface-expos ed residues in a direction perpendicular to the membrane is similar to that in helical membrane proteins, with aliphatic residues concentrat ed in the central 20 Angstrom of the bilayer. Outside these residues i s a layer of aromatic residues, followed by polar and charged residues . Residues in the trimer interface are more conserved than residues no t in the interface. By comparing the interface and noninterface residu es, an interface preference scale has been derived that may be used as a basis for predicting interface surfaces in monomer models.