title: Structural determinants of TRIM protein function.
abstract: Tripartite motif (TRIM) proteins constitute one of the largest subfamilies of Really Interesting New Gene (RING) E3 ubiquitin ligases and contribute to the regulation of numerous cellular activities, including innate immune responses. The conserved TRIM harbours a RING domain that imparts E3 ligase activity to TRIM family proteins, whilst a variable C-terminal region can mediate recognition of substrate proteins. The knowledge of the structure of these multidomain proteins and the functional interplay between their constituent domains is paramount to understanding their cellular roles. To date, available structural information on TRIM proteins is still largely restricted to subdomains of many TRIMs in isolation. Nevertheless, applying a combination of structural, biophysical and biochemical approaches has recently allowed important progress to be made towards providing a better understanding of the molecular features that underlie the function of TRIM family proteins and has uncovered an unexpected diversity in the link between self-association and catalytic activity.
authors.affiliation: Molecular Structure of Cell Signalling Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, U.K.
authors.forename: Diego
authors.initials: D
authors.lastname: Esposito
authors.affiliation: Molecular Structure of Cell Signalling Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, U.K.
authors.forename: Marios G
authors.initials: MG
authors.lastname: Koliopoulos
authors.affiliation: Molecular Structure of Cell Signalling Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, U.K. katrin.rittinger@crick.ac.uk.
authors.forename: Katrin
authors.initials: K
authors.lastname: Rittinger
mesh_terms: D000818:Animals; D055162:Biocatalysis; D006801:Humans; D008958:Models, Molecular; D005810:Multigene Family; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D054829:RING Finger Domains; D000070584:Tripartite Motif Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D044767:Ubiquitin-Protein Ligases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D000070584:Tripartite Motif Proteins; D044767:Ubiquitin-Protein Ligases
keywords: structural characterisation; ubiquitin ligases; ubiquitin signalling