ArticleProtein science : a publication of the Protein Society2007
The Abl SH2-kinase linker naturally adopts a conformation competent for SH3 domain binding.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Review
- Protein conformational ensembles in function: roles and mechanisms.RSC chemical biology · 2023Review
- Allosteric regulation of autoinhibition and activation of c-Abl.Computational and structural biotechnology journal · 2022Article
- Coupled regulation by the juxtamembrane and sterile α motif (SAM) linker is a hallmark of ephrin tyrosine kinase evolution.The Journal of biological chemistry · 2018Article
- Atomic view of the energy landscape in the allosteric regulation of Abl kinase.Nature structural & molecular biology · 2017Article
- Iminoguanidines as Allosteric Inhibitors of the Iron-Regulated Heme Oxygenase (HemO) of Pseudomonas aeruginosa.Journal of medicinal chemistry · 2016Article
- Dynamics of the Tec-family tyrosine kinase SH3 domains.Protein science : a publication of the Protein Society · 2016Article
- Misfolding, Aggregation, and Disordered Segments in c-Abl and p53 in Human Cancer.Frontiers in oncology · 2015Review
- Fluorescence Polarization Screening Assays for Small Molecule Allosteric Modulators of ABL Kinase Function.PloS one · 2015Article
- Analytical Aspects of Hydrogen Exchange Mass Spectrometry.Annual review of analytical chemistry (Palo Alto, Calif.) · 2015Review
- Conformational analysis of processivity clamps in solution demonstrates that tertiary structure does not correlate with protein dynamics.Structure (London, England : 1993) · 2014Article
- Two-state dynamics of the SH3-SH2 tandem of Abl kinase and the allosteric role of the N-cap.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Structure and dynamic regulation of Abl kinases.The Journal of biological chemistry · 2013Review
- Protein conformation ensembles monitored by HDX reveal a structural rationale for abscisic acid signaling protein affinities and activities.Structure (London, England : 1993) · 2013Article
- Partial cooperative unfolding in proteins as observed by hydrogen exchange mass spectrometry.International reviews in physical chemistry · 2013Article
- What's in a loop?Cell communication and signaling : CCS · 2012Article
- Conformational transitions in the membrane scaffold protein of phospholipid bilayer nanodiscs.Molecular & cellular proteomics : MCP · 2011Article
- On the solution conformation and dynamics of the HIV-1 viral infectivity factor.Journal of molecular biology · 2011Article
- Differential hydrogen/deuterium exchange mass spectrometry analysis of protein-ligand interactions.Expert review of proteomics · 2011Review
- Hierarchical modeling of activation mechanisms in the ABL and EGFR kinase domains: thermodynamic and mechanistic catalysts of kinase activation by cancer mutations.PLoS computational biology · 2009Article
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4 authors.
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Abstract
The core of the Abelson tyrosine kinase (c-Abl) is structurally similar to Src-family kinases where SH3 and SH2 domains pack against the backside of the kinase domain in the down-regulated conformation. Both kinase families depend upon intramolecular association of SH3 with the linker joining the SH2 and kinase domains for suppression of kinase activity. Hydrogen deuterium exchange (HX) and mass spectrometry (MS) were used to probe intramolecular interaction of the c-Abl SH3 domain with the linker in recombinant constructs lacking the kinase domain. Under physiological conditions, the c-Abl SH3 domain undergoes partial unfolding, which is stabilized by ligand binding, providing a unique assay for SH3:linker interaction in solution. Using this approach, we observed dynamic association of the SH3 domain with the linker in the absence of the kinase domain. Truncation of the linker before W254 completely prevented cis-interaction with SH3, while constructs containing amino acids past this point showed SH3:linker interactions. The observation that the Abl linker sequence exhibits SH3-binding activity in the absence of the kinase domain is unique to Abl and was not observed with Src-family kinases. These results suggest that SH3:linker interactions may have a more prominent role in Abl regulation than in Src kinases, where the down-regulated conformation is further stabilized by a second intramolecular interaction between the C-terminal tail and the SH2 domain.
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