ArticleJournal of molecular modeling2009
An interrupted beta-propeller and protein disorder: structural bioinformatics insights into the N-terminus of alsin.
Article in Journal of molecular modeling, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Review
- Personalized Treatment for Infantile Ascending Hereditary Spastic Paralysis Based on In Silico Strategies.Molecules (Basel, Switzerland) · 2022Article
- Review
- In silico investigation of Alsin RLD conformational dynamics and phosphoinositides binding mechanism.PloS one · 2022Article
- Prediction of Protein-Protein Interactions Between Alsin DH/PH and Rac1 and Resulting Protein Dynamics.Frontiers in molecular neuroscience · 2021Article
- Altered oligomeric states in pathogenic ALS2 variants associated with juvenile motor neuron diseases cause loss of ALS2-mediated endosomal function.The Journal of biological chemistry · 2018Article
- A novel mutation causing nephronophthisis in the Lewis polycystic kidney rat localises to a conserved RCC1 domain in Nek8.BMC genomics · 2012Article
- Identification and structural characterization of FYVE domain-containing proteins of Arabidopsis thaliana.BMC plant biology · 2010Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Defects in the human ALS2 gene, which encodes the 1,657-amino-acid residue protein alsin, are linked to several related motor neuron diseases. We created a structural model for the N-terminal 690-residue region of alsin through comparative modelling based on regulator of chromosome condensation 1 (RCC1). We propose that this alsin region contains seven RCC1-like repeats in a seven-bladed beta-propeller structure. The propeller is formed by a double clasp arrangement containing two segments (residues 1-218 and residues 525-690). The 306-residue insert region, predicted to lie within blade 5 and to be largely disordered, is poorly conserved across species. Surface patches of evolutionary conservation probably indicate locations of binding sites. Both disease-causing missense mutations-Cys157Tyr and Gly540Glu-are buried in the propeller and likely to be structurally disruptive. This study aids design of experimental studies by highlighting the importance of construct length, will enhance interpretation of protein-protein interactions, and enable rational site-directed mutagenesis.
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