Sequence and structural analysis of BTB domain proteins

By P. Stogios, Gregory S. Downs, Jimmy JS Jauhal, Sukhjeen K Nandra, G. Privé. Genome Biology, 2005

703 citations recorded by the source corpus.

BackgroundThe 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.ResultsWe 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.ConclusionDespite 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.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/d0aaf7b57ff43dccf08b41041b255c60e14bf72d

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Citations in the corpus

Keap1 Recruits Neh2 through Binding to ETGE and DLG Motifs: Characterization of the Two-Site Molecular Recognition Model (2006, background): “Except for the DDB1, core BTB folds are found in SKP1, Elongin C and other BTB proteins (54).”
The integrated landscape of driver genomic alterations in glioblastoma (2013, background): “The model does not include higher quaternary structure, although many BTB domains, and many kelch domains, are known to self associate 25 .”
Mutations in Kelch-like 3 and Cullin 3 cause hypertension and electrolyte abnormalities (2012, background): “D413G (de novo); aka ES enhancer a(5)g L D K”
Genome-Wide and Functional Annotation of Human E3 Ubiquitin Ligases Identifies MULAN, a Mitochondrial E3 that Regulates the Organelle's Dynamics and Signaling (2008, background): “. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . Protein family Gene name Gene symbol Ubox PRP19 YLL036C UFD2 YDL190C HECT TOM1 YDR457W HUL4 YJR036C HUL5 YGL141W UFD4 YKL010C RSP5 YER125W F BOX COS111 YBR203W ”