Structural modeling of ataxin‐3 reveals distant homology to adaptins
Identifieur interne : 000B52 ( Main/Exploration ); précédent : 000B51; suivant : 000B53Structural modeling of ataxin‐3 reveals distant homology to adaptins
Auteurs : Mario Albrecht [Allemagne] ; Daniel Hoffmann [Allemagne] ; Bernd O. Evert [Allemagne] ; Ina Schmitt [Allemagne] ; Ullrich Wüllner [Allemagne] ; Thomas Lengauer [Allemagne]Source :
- Proteins: Structure, Function, and Bioinformatics [ 0887-3585 ] ; 2003-02-01.
English descriptors
- KwdEn :
- Teeft :
- Acad, Academic press, Accession, Accession numbers, Adaptin, Adaptins, Albrecht, Alignment, Alignment columns, Amidation, Amidation pattern, Amino acids, Amyloid, Amyloid formation, Ataxia, Biol, Biol cell, Biol chem, Cell biol, Cell death, Cerebellar ataxias, Chicken homolog, Clathrin, Clustal, Complementary methods, Conf intell syst, Crystal structure, Curr, Curr biol, Curr opin cell biol, Curr opin struct biol, Database, Database searches, Different species, Distant homology, Distant relationship, Domain, Domain architectures, Domain proteins, Drosophila, Eisenberg, Endocytic proteins, Endocytosis, Ent1, Enth, Enth domain, Epsin, Epsin homology, Equivalence threshold, Eukaryotic cells, Experimental data, Feb, Febs lett, Functional hypotheses, Functional relevance, Further experiments, Gene expression atlas8, Genet, Genome, Glutamine, Helix, Helix bundles, High probability, Homolog, Homologs, Homology, Human homologs, Human josephin, Human tom1, Important role, Intranuclear inclusions, Josephin, Josephin domain, Lett, Long helix, Markov models, Meta server, Modeling, Molecular aspects, Monomeric adaptins, Mouse josephin, Multicoil, Multiple alignment, Multiple sequence alignment, Multiple sequence alignments, Natl, Neurodegenerative, Neurodegenerative disease, Neurodegenerative diseases, Nuclear hormone receptors, Nuclear inclusions, Nuclear matrix, Nuclear receptor coactivators, Nucleic, Nucleic acids, Other proteins, Overall structure, Pathogenic, Pathogenic forms, Paulson, Perutz, Pfam, Pfam database, Polar zippers, Polyglutamine, Polyglutamine disease, Polyglutamine diseases, Polyglutamine region, Polyglutamine tract, Predictive strategy, Proc, Proc natl acad, Protein, Protein aggregation, Protein complexes, Protein data bank, Protein sequences, Protein structures, Protein variant, Putative, Putative region, Receptor, Receptor endocytosis, Recognition tools, Remote homology, Repair protein, Respective proteins, Sankt augustin, Schloss birlinghoven, Scop database, Second protein, Secondary structure, Secondary structure assignments, Secondary structure prediction, Secondary structure predictions, Secondary structures, Sequence accession numbers, Sequence identity, Sequence motifs, Sequence part, Sequence parts, Sequence regions, Sequence rest, Server, Several regions, Shorter sequence, Similar domain architectures, Similar results, Spectrin domain, Spinocerebellar, Spinocerebellar ataxia, Spinocerebellar ataxia type, Sspro, Stat proteins, Struct, Struct biol, Structural basis, Structural model, Structural modeling, Structure prediction, Subunit, Superposition program, Thaliana, Thaliana homolog, Transcription, Transcriptional, Trends biochem, Ubiq domain, Unknown function, Unstructured proteins, Yeast, Yeast ggas.
Abstract
Spinocerebellar ataxia type 3 (SCA3) is a polyglutamine disorder caused by a CAG repeat expansion in the coding region of a gene encoding ataxin‐3, a protein of yet unknown function. Based on a comprehensive computational analysis, we propose a structural model and structure‐based functions for ataxin‐3. Our predictive strategy comprises the compilation of multiple sequence and structure alignments of carefully selected proteins related to ataxin‐3. These alignments are consistent with additional information on sequence motifs, secondary structure, and domain architectures. The application of complementary methods revealed the homology of ataxin‐3 to ENTH and VHS domain proteins involved in membrane trafficking and regulatory adaptor functions. We modeled the structure of ataxin‐3 using the adaptin AP180 as a template and assessed the reliability of the model by comparison with known sequence and structural features. We could further infer potential functions of ataxin‐3 in agreement with known experimental data. Our database searches also identified an as yet uncharacterized family of proteins, which we named josephins because of their pronounced homology to the Josephin domain of ataxin‐3. Proteins 2003;50:355–370. © 2002 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/prot.10280
Affiliations:
- Allemagne
- District de Cologne, Rhénanie-du-Nord-Westphalie, Sarre (Land)
- Bonn, Sankt Augustin, Sarrebruck
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<front><div type="abstract" xml:lang="en">Spinocerebellar ataxia type 3 (SCA3) is a polyglutamine disorder caused by a CAG repeat expansion in the coding region of a gene encoding ataxin‐3, a protein of yet unknown function. Based on a comprehensive computational analysis, we propose a structural model and structure‐based functions for ataxin‐3. Our predictive strategy comprises the compilation of multiple sequence and structure alignments of carefully selected proteins related to ataxin‐3. These alignments are consistent with additional information on sequence motifs, secondary structure, and domain architectures. The application of complementary methods revealed the homology of ataxin‐3 to ENTH and VHS domain proteins involved in membrane trafficking and regulatory adaptor functions. We modeled the structure of ataxin‐3 using the adaptin AP180 as a template and assessed the reliability of the model by comparison with known sequence and structural features. We could further infer potential functions of ataxin‐3 in agreement with known experimental data. Our database searches also identified an as yet uncharacterized family of proteins, which we named josephins because of their pronounced homology to the Josephin domain of ataxin‐3. Proteins 2003;50:355–370. © 2002 Wiley‐Liss, Inc.</div>
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