Cargando…

Sequence and structural analysis of BTB domain proteins

BACKGROUND: The BTB domain (also known as the POZ domain) is a versatile protein-protein interaction motif that participates in a wide range of cellular functions, including transcriptional regulation, cytoskeleton dynamics, ion channel assembly and gating, and targeting proteins for ubiquitination....

Descripción completa

Detalles Bibliográficos
Autores principales: Stogios, Peter J, Downs, Gregory S, Jauhal, Jimmy JS, Nandra, Sukhjeen K, Privé, Gilbert G
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1257465/
https://www.ncbi.nlm.nih.gov/pubmed/16207353
http://dx.doi.org/10.1186/gb-2005-6-10-r82
_version_ 1782125813235187712
author Stogios, Peter J
Downs, Gregory S
Jauhal, Jimmy JS
Nandra, Sukhjeen K
Privé, Gilbert G
author_facet Stogios, Peter J
Downs, Gregory S
Jauhal, Jimmy JS
Nandra, Sukhjeen K
Privé, Gilbert G
author_sort Stogios, Peter J
collection PubMed
description BACKGROUND: The BTB domain (also known as the POZ domain) is a versatile protein-protein interaction motif that participates in a wide range of cellular functions, including transcriptional regulation, cytoskeleton dynamics, ion channel assembly and gating, and targeting proteins for ubiquitination. Several BTB domain structures have been experimentally determined, revealing a highly conserved core structure. RESULTS: We surveyed the protein architecture, genomic distribution and sequence conservation of BTB domain proteins in 17 fully sequenced eukaryotes. The BTB domain is typically found as a single copy in proteins that contain only one or two other types of domain, and this defines the BTB-zinc finger (BTB-ZF), BTB-BACK-kelch (BBK), voltage-gated potassium channel T1 (T1-Kv), MATH-BTB, BTB-NPH3 and BTB-BACK-PHR (BBP) families of proteins, among others. In contrast, the Skp1 and ElonginC proteins consist almost exclusively of the core BTB fold. There are numerous lineage-specific expansions of BTB proteins, as seen by the relatively large number of BTB-ZF and BBK proteins in vertebrates, MATH-BTB proteins in Caenorhabditis elegans, and BTB-NPH3 proteins in Arabidopsis thaliana. Using the structural homology between Skp1 and the PLZF BTB homodimer, we present a model of a BTB-Cul3 SCF-like E3 ubiquitin ligase complex that shows that the BTB dimer or the T1 tetramer is compatible in this complex. CONCLUSION: Despite widely divergent sequences, the BTB fold is structurally well conserved. The fold has adapted to several different modes of self-association and interactions with non-BTB proteins.
format Text
id pubmed-1257465
institution National Center for Biotechnology Information
language English
publishDate 2005
publisher BioMed Central
record_format MEDLINE/PubMed
spelling pubmed-12574652005-10-19 Sequence and structural analysis of BTB domain proteins Stogios, Peter J Downs, Gregory S Jauhal, Jimmy JS Nandra, Sukhjeen K Privé, Gilbert G Genome Biol Research BACKGROUND: The BTB domain (also known as the POZ domain) is a versatile protein-protein interaction motif that participates in a wide range of cellular functions, including transcriptional regulation, cytoskeleton dynamics, ion channel assembly and gating, and targeting proteins for ubiquitination. Several BTB domain structures have been experimentally determined, revealing a highly conserved core structure. RESULTS: We surveyed the protein architecture, genomic distribution and sequence conservation of BTB domain proteins in 17 fully sequenced eukaryotes. The BTB domain is typically found as a single copy in proteins that contain only one or two other types of domain, and this defines the BTB-zinc finger (BTB-ZF), BTB-BACK-kelch (BBK), voltage-gated potassium channel T1 (T1-Kv), MATH-BTB, BTB-NPH3 and BTB-BACK-PHR (BBP) families of proteins, among others. In contrast, the Skp1 and ElonginC proteins consist almost exclusively of the core BTB fold. There are numerous lineage-specific expansions of BTB proteins, as seen by the relatively large number of BTB-ZF and BBK proteins in vertebrates, MATH-BTB proteins in Caenorhabditis elegans, and BTB-NPH3 proteins in Arabidopsis thaliana. Using the structural homology between Skp1 and the PLZF BTB homodimer, we present a model of a BTB-Cul3 SCF-like E3 ubiquitin ligase complex that shows that the BTB dimer or the T1 tetramer is compatible in this complex. CONCLUSION: Despite widely divergent sequences, the BTB fold is structurally well conserved. The fold has adapted to several different modes of self-association and interactions with non-BTB proteins. BioMed Central 2005 2005-09-15 /pmc/articles/PMC1257465/ /pubmed/16207353 http://dx.doi.org/10.1186/gb-2005-6-10-r82 Text en Copyright © 2005 Stogios et al.; licensee BioMed Central Ltd.
spellingShingle Research
Stogios, Peter J
Downs, Gregory S
Jauhal, Jimmy JS
Nandra, Sukhjeen K
Privé, Gilbert G
Sequence and structural analysis of BTB domain proteins
title Sequence and structural analysis of BTB domain proteins
title_full Sequence and structural analysis of BTB domain proteins
title_fullStr Sequence and structural analysis of BTB domain proteins
title_full_unstemmed Sequence and structural analysis of BTB domain proteins
title_short Sequence and structural analysis of BTB domain proteins
title_sort sequence and structural analysis of btb domain proteins
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1257465/
https://www.ncbi.nlm.nih.gov/pubmed/16207353
http://dx.doi.org/10.1186/gb-2005-6-10-r82
work_keys_str_mv AT stogiospeterj sequenceandstructuralanalysisofbtbdomainproteins
AT downsgregorys sequenceandstructuralanalysisofbtbdomainproteins
AT jauhaljimmyjs sequenceandstructuralanalysisofbtbdomainproteins
AT nandrasukhjeenk sequenceandstructuralanalysisofbtbdomainproteins
AT privegilbertg sequenceandstructuralanalysisofbtbdomainproteins