Top surface blade residues and the central channel water molecules are conserved in every repeat of the integrin-like β-propeller structures.

A1 Journal article (refereed)


Internal Authors/Editors


Publication Details

List of Authors: Denesyuk A, Denessiouk K, Johnson MS.
Publisher: Academic Press
Place: Netherlands
Publication year: 2018
Journal: Journal of Structural Biology
Journal acronym: JSB
Volume number: 201
Issue number: 2
Start page: 155
End page: 161
eISSN: 1095-8657


Abstract

An integrin-like β-propeller domain contains seven repeats of a
four-stranded antiparallel β-sheet motif (blades). Previously we
described a 3D structural motif within each blade of the integrin-type
β-propeller. Here, we show unique structural links that join different
blades of the β-propeller structure, which together with the structural
motif for a single blade are repeated in a β-propeller to provide the
functional top face of the barrel, found to be involved in
protein-protein interactions and substrate recognition. We compare
functional top face diagrams of the integrin-type β-propeller domain and
two non-integrin type β-propeller domains of virginiamycin B lyase and
WD Repeat-Containing Protein 5.


Keywords

bioinformatics, integrins, protein structure motifs

Last updated on 2019-16-10 at 03:19