ArticleProceedings of the National Academy of Sciences of the United States of America1997
Human argininosuccinate lyase: a structural basis for intragenic complementation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed, 91 citations in OpenAlex.
- Predicting epistasis across proteins by structural logic.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Clinical, biochemical and genetic characteristics of patients with argininosuccinate lyase deficiency from a single center cohort in China.Orphanet journal of rare diseases · 2025Article
- Arginine inhibition of the argininosuccinate lyases is conserved among three orders in cyanobacteria.Plant molecular biology · 2022Article
- What Genetics Has Told Us and How It Can Inform Future Experiments for Spinal Muscular Atrophy, a Perspective.International journal of molecular sciences · 2021Article
- Identification of rare variants causing urea cycle disorders: A clinical, genetic, and biophysical study.Journal of cellular and molecular medicine · 2021Article
- Conditional deletion of SMN in cell culture identifies functional SMN alleles.Human molecular genetics · 2020Article
- Enzymes Involved in the Biosynthesis of Arginine from Ornithine in Maritime Pine (Plants (Basel, Switzerland) · 2020Article
- Identification of mutations in Malaysian patients with argininosuccinate lyase (ASL) deficiency.Molecular genetics and metabolism reports · 2019Article
- Phosphatidylinositol 4,5-Bisphosphate-Dependent Oligomerization of the Pseudomonas aeruginosa Cytotoxin ExoU.Infection and immunity · 2018Article
- Effect of Cysteamine on Mutant ASL Proteins with Cysteine for Arginine Substitutions.Molecular diagnosis & therapy · 2016Article
- Article
- xMDFF: molecular dynamics flexible fitting of low-resolution X-ray structures.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Cloning, expression, purification, crystallization and preliminary X-ray studies of argininosuccinate lyase (Rv1659) from Mycobacterium tuberculosis.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Understanding the role of argininosuccinate lyase transcript variants in the clinical and biochemical variability of the urea cycle disorder argininosuccinic aciduria.The Journal of biological chemistry · 2013Article
- Proteomic analysis of immediate-early response plasma proteins after 70% and 90% partial hepatectomy.Hepatology research : the official journal of the Japan Society of Hepatology · 2013Article
- Optimizing therapy for argininosuccinic aciduria.Molecular genetics and metabolism · 2012Review
- Argininosuccinate lyase deficiency.Genetics in medicine : official journal of the American College of Medical Genetics · 2012Review
- Genetic control of seed shattering in rice by the APETALA2 transcription factor shattering abortion1.The Plant cell · 2012Article
- Argininosuccinate lyase deficiency-argininosuccinic aciduria and beyond.American journal of medical genetics. Part C, Seminars in medical genetics · 2011Review
- Novel mutations underlying argininosuccinic aciduria in Saudi Arabia.BMC research notes · 2010Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intragenic complementation has been observed at the argininosuccinate lyase (ASL) locus. Intragenic complementation is a phenomenon that occurs when a multimeric protein is formed from subunits produced by different mutant alleles of a gene. The resulting hybrid protein exhibits enzymatic activity that is greater than that found in the oligomeric proteins produced by each mutant allele alone. The mutations involved in the most successful complementation event observed in ASL deficiency were found to be an aspartate to glycine mutation at codon 87 of one allele (D87G) coupled with a glutamine to arginine mutation at codon 286 of the other (Q286R). To understand the structural basis of the Q286R:D87G intragenic complementation event at the ASL locus, we have determined the x-ray crystal structure of recombinant human ASL at 4. 0 A resolution. The structure has been refined to an R factor of 18. 8%. Two monomers related by a noncrystallographic 2-fold axis comprise the asymmetric unit, and a crystallographic 2-fold axis of space group P3121 completes the tetramer. Each of the four active sites is composed of residues from three monomers. Structural mapping of the Q286R and D87G mutations indicate that both are near the active site and each is contributed by a different monomer. Thus when mutant monomers combine randomly such that one active site contains both mutations, it is required by molecular symmetry that another active site exists with no mutations. These "native" active sites give rise to the observed partial recovery of enzymatic activity.
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