ArticlePloS one2011
Mutations in the catalytic loop HRD motif alter the activity and function of Drosophila Src64.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 28 citations in OpenAlex.
- Dynamic structural profiling of PINK1 mutations (T313M and L347P) reveals a vital molecular perturbation namely phospho-Serine 65 ubiquitin recognition point in mitophagy mediated autosomal recessive Parkinson's disease (ARPD).Frontiers in molecular neuroscience · 2026Article
- The novel HRD motif kinase SPE-60 is required for sperm development and motility in Caenorhabditis elegans.Scientific reports · 2025Article
- Exploring protein adenylyltransferase as a therapeutic target for combating ESKAPE pathogens in hospital-acquired infections.Molecular biology reports · 2025Review
- Expression, Purification and Biophysical Characterisation of Klebsiella Pneumoniae Protein Adenylyltransferase: A Systematic Integration of Empirical and Computational Modelling Approaches.The protein journal · 2024Article
- Modulation of IRAK enzymes as a therapeutic strategy against SARS-CoV-2 induced cytokine storm.Clinical and experimental medicine · 2023Review
- Comparative analysis of the kinomes of Plasmodium falciparum, Plasmodium vivax and their host Homo sapiens.BMC genomics · 2022Article
- Back From the Dead: The Atypical Kinase Activity of a Pseudokinase Regulator of Cation Fluxes During Inducible Immunity.Frontiers in plant science · 2022Article
- Structural versatility that serves the function of the HRD motif in the catalytic loop of protein tyrosine kinase, Src.Protein science : a publication of the Protein Society · 2019Article
- C-terminal Src kinase (Csk) regulates the tricellular junction protein Gliotactin independent of Src.Molecular biology of the cell · 2018Article
- Kinetic and structural analyses reveal residues in phosphoinositide 3-kinase α that are critical for catalysis and substrate recognition.The Journal of biological chemistry · 2017Article
- Article
- HUMAN KINASES DISPLAY MUTATIONAL HOTSPOTS AT COGNATE POSITIONS WITHIN CANCER.Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing · 2017Article
- Drak Is Required for Actomyosin Organization During Drosophila Cellularization.G3 (Bethesda, Md.) · 2016Article
- Locking the active conformation of c-Src kinase through the phosphorylation of the activation loop.Journal of molecular biology · 2014Article
- Article
- Deciphering the structural basis of eukaryotic protein kinase regulation.PLoS biology · 2013Article
- Identification of a hidden strain switch provides clues to an ancient structural mechanism in protein kinases.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The catalytic loop HRD motif is found in most protein kinases and these amino acids are predicted to perform functions in catalysis, transition to, and stabilization of the active conformation of the kinase domain. We have identified mutations in a Drosophila src gene, src64, that alter the three HRD amino acids. We have analyzed the mutants for both biochemical activity and biological function during development. Mutation of the aspartate to asparagine eliminates biological function in cytoskeletal processes and severely reduces fertility, supporting the amino acid's critical role in enzymatic activity. The arginine to cysteine mutation has little to no effect on kinase activity or cytoskeletal reorganization, suggesting that the HRD arginine may not be critical for coordinating phosphotyrosine in the active conformation. The histidine to leucine mutant retains some kinase activity and biological function, suggesting that this amino acid may have a biochemical function in the active kinase that is independent of its side chain hydrogen bonding interactions in the active site. We also describe the phenotypic effects of other mutations in the SH2 and tyrosine kinase domains of src64, and we compare them to the phenotypic effects of the src64 null allele.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.