ArticleJournal of molecular biology2007
A novel disulfide bond in the SH2 Domain of the C-terminal Src kinase controls catalytic activity.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- DYT8 drives lung adenocarcinoma through EGFR-mediated PSMC6 recruitment and uncharacterized phosphorylation at Ser 306 and 525 of c-Src.Acta pharmacologica Sinica · 2026Article
- CSK-mediated signalling by integrins in cancer.Frontiers in cell and developmental biology · 2023Review
- Dissection of the catalytic and regulatory structure-function relationships of Csk protein tyrosine kinase.Frontiers in cell and developmental biology · 2023Review
- The reduced form of the antibody CH2 domain.Protein science : a publication of the Protein Society · 2021Article
- Redox regulation of tyrosine kinase signalling: more than meets the eye.Journal of biochemistry · 2020Review
- Cysteines and Disulfide Bonds as Structure-Forming Units: Insights From Different Domains of Life and the Potential for Characterization by NMR.Frontiers in chemistry · 2020Review
- SUMOylation of Csk Negatively Modulates its Tumor Suppressor Function.Neoplasia (New York, N.Y.) · 2019Article
- Oxidative Stress-Driven Autophagy acROSs Onset and Therapeutic Outcome in Hepatocellular Carcinoma.Oxidative medicine and cellular longevity · 2019Review
- ROS-dependent activation of RhoA/Rho-kinase in pulmonary artery: Role of Src-family kinases and ARHGEF1.Free radical biology & medicine · 2017Article
- Redox regulation of the actin cytoskeleton and its role in the vascular system.Free radical biology & medicine · 2017Review
- Combining biophysical methods to analyze the disulfide bond in SH2 domain of C-terminal Src kinase.Biophysics reports · 2016Article
- Control of vascular smooth muscle function by Src-family kinases and reactive oxygen species in health and disease.The Journal of physiology · 2015Review
- TGFβ1 rapidly activates Src through a non-canonical redox signaling mechanism.Archives of biochemistry and biophysics · 2015Article
- The role of Nox-mediated oxidation in the regulation of cytoskeletal dynamics.Current pharmaceutical design · 2015Review
- Solubility of recombinant Src homology 2 domains expressed in E. coli can be predicted by TANGO.BMC biotechnology · 2014Article
- Targeting allosteric disulphide bonds in cancer.Nature reviews. Cancer · 2013Review
- Simple approach to assign disulfide connectivity using extracted ion chromatograms of electron transfer dissociation spectra.Analytical chemistry · 2013Article
- Distal loop flexibility of a regulatory domain modulates dynamics and activity of C-terminal SRC kinase (csk).PLoS computational biology · 2013Article
- Cigarette smoke extract stimulates epithelial-mesenchymal transition through Src activation.Free radical biology & medicine · 2012Article
- Regulation of the SRC family kinases by Csk.International journal of biological sciences · 2012Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The SH2 domain of the C-terminal Src kinase [Csk] contains a unique disulfide bond that is not present in other known SH2 domains. To investigate whether this unusual disulfide bond serves a novel function, the effects of disulfide bond formation on catalytic activity of the full-length protein and on the structure of the SH2 domain were investigated. The kinase activity of full-length Csk decreases by an order of magnitude upon formation of the disulfide bond in the distal SH2 domain. NMR spectra of the fully oxidized and fully reduced SH2 domains exhibit similar chemical shift patterns and are indicative of similar, well-defined tertiary structures. The solvent-accessible disulfide bond in the isolated SH2 domain is highly stable and far from the small lobe of the kinase domain. However, reduction of this bond results in chemical shift changes of resonances that map to a cluster of residues that extend from the disulfide bond across the molecule to a surface that is in direct contact with the small lobe of the kinase domain in the intact molecule. Normal mode analyses and molecular dynamics calculations suggest that disulfide bond formation has large effects on residues within the kinase domain, most notably within the active-site cleft. Overall, the data indicate that reversible cross-linking of two cysteine residues in the SH2 domain greatly impacts catalytic function and interdomain communication in Csk.
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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.