ArticleProceedings of the National Academy of Sciences of the United States of America2005
Crystal structure of the GTPase domain of rat dynamin 1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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Who cites it
34 citing papers in PubMed, 68 citations in OpenAlex.
- Structural basis for regulated assembly of the mitochondrial fission GTPase Drp1.Nature communications · 2024Article
- Cellular and structural insight into dynamin function during endocytic vesicle formation: a tale of 50 years of investigation.Bioscience reports · 2022Review
- Centronuclear Myopathy Caused by Defective Membrane Remodelling of Dynamin 2 and BIN1 Variants.International journal of molecular sciences · 2022Review
- Unraveling a Force-Generating Allosteric Pathway of Actomyosin Communication Associated with ADP and PInternational journal of molecular sciences · 2020Article
- Structural and Computational Insights into a Blebbistatin-Bound Myosin•ADP Complex with Characteristics of an ADP-Release Conformation along the Two-Step Myosin Power Stoke.International journal of molecular sciences · 2020Article
- The structural biology of the dynamin-related proteins: New insights into a diverse, multitalented family.Traffic (Copenhagen, Denmark) · 2019Review
- Regulation of dynamin family proteins by post-translational modifications.Journal of biosciences · 2017Review
- Structure of actomyosin rigour complex at 5.2 Å resolution and insights into the ATPase cycle mechanism.Nature communications · 2017Article
- Article
- Deformable elastic network refinement for low-resolution macromolecular crystallography.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Synthesis of Dynole 34-2, Dynole 2-24 and Dyngo 4a for investigating dynamin GTPase.Nature protocols · 2014Article
- Dynamin-2 function and dysfunction along the secretory pathway.Frontiers in endocrinology · 2013Review
- MCPath: Monte Carlo path generation approach to predict likely allosteric pathways and functional residues.Nucleic acids research · 2013Article
- Building a fission machine--structural insights into dynamin assembly and activation.Journal of cell science · 2013Review
- Functional mapping of human dynamin-1-like GTPase domain based on x-ray structure analyses.PloS one · 2013Article
- Mechanics of dynamin-mediated membrane fission.Annual review of biophysics · 2013Review
- Dynamin and PTP-PEST cooperatively regulate Pyk2 dephosphorylation in osteoclasts.The international journal of biochemistry & cell biology · 2012Article
- A pseudoatomic model of the dynamin polymer identifies a hydrolysis-dependent powerstroke.Cell · 2011Article
- The crystal structure of dynamin.Nature · 2011Article
- Crystal structure of nucleotide-free dynamin.Nature · 2011Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Here, we present the 1.9-A crystal structure of the nucleotide-free GTPase domain of dynamin 1 from Rattus norvegicus. The structure corresponds to an extended form of the canonical GTPase fold observed in Ras proteins. Both nucleotide-binding switch motifs are well resolved, adopting conformations that closely resemble a GTP-bound state not previously observed for nucleotide-free GTPases. Two highly conserved arginines, Arg-66 and Arg-67, greatly restrict the mobility of switch I and are ideally positioned to relay information about the nucleotide state to other parts of the protein. Our results support a model in which switch I residue Arg-59 gates GTP binding in an assembly-dependent manner and the GTPase effector domain functions as an assembly-dependent GTPase activating protein in the fashion of RGS-type GAPs.
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Registered trials
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.