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

A1 Originalartikel i en vetenskaplig tidskrift (referentgranskad)


Interna författare/redaktörer


Publikationens författare: Denesyuk A, Denessiouk K, Johnson MS.
Förläggare: Academic Press
Förlagsort: Netherlands
Publiceringsår: 2018
Tidskrift: Journal of Structural Biology
Tidskriftsakronym: JSB
Volym: 201
Nummer: 2
Artikelns första sida, sidnummer: 155
Artikelns sista sida, sidnummer: 161
eISSN: 1095-8657


Abstrakt

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.


Nyckelord

bioinformatics, integrins, protein structure motifs

Senast uppdaterad 2019-26-06 vid 05:28