ArticleBiochemistry2006
Solution structure and folding characteristics of the C-terminal SH3 domain of c-Crk-II.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 45 citations in OpenAlex.
- Crk proteins activate the Rap1 guanine nucleotide exchange factor C3G by segregated adaptor-dependent and -independent mechanisms.Cell communication and signaling : CCS · 2023Article
- Chemoenzymatic Semisynthesis of Proteins.Chemical reviews · 2020Review
- Article
- Article
- Prolyl isomerization as a molecular memory in the allosteric regulation of the signal adapter protein c-CrkII.The Journal of biological chemistry · 2015Article
- The Role of Crk Adaptor Proteins in T-Cell Adhesion and Migration.Frontiers in immunology · 2015Review
- Molecular dynamics of the proline switch and its role in Crk signaling.The journal of physical chemistry. B · 2014Article
- Contribution of Crk adaptor proteins to host cell and bacteria interactions.BioMed research international · 2014Review
- The adaptor protein Crk in immune response.Immunology and cell biology · 2014Review
- SH3 domains: modules of protein-protein interactions.Biophysical reviews · 2013Review
- Domain organization differences explain Bcr-Abl's preference for CrkL over CrkII.Nature chemical biology · 2012Article
- Models of crk adaptor proteins in cancer.Genes & cancer · 2012Article
- Roles for crk in cancer metastasis and invasion.Genes & cancer · 2012Article
- Phosphorylation of Crk on tyrosine 251 in the RT loop of the SH3C domain promotes Abl kinase transactivation.Oncogene · 2011Article
- CrkL is a co-activator of estrogen receptor alpha that enhances tumorigenic potential in cancer.Molecular endocrinology (Baltimore, Md.) · 2011Article
- Domain cooperativity in multidomain proteins: what can we learn from molecular alignment in anisotropic media?Journal of biomolecular NMR · 2011Article
- Tuning protein autoinhibition by domain destabilization.Nature structural & molecular biology · 2011Article
- Structural basis for regulation of the Crk signaling protein by a proline switch.Nature chemical biology · 2011Article
- Emerging roles for crk in human cancer.Genes & cancer · 2010Article
- Structural determination of biomolecular interfaces by nuclear magnetic resonance of proteins with reduced proton density.Journal of biomolecular NMR · 2010Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Crk-II is a signaling adaptor protein that is involved in many cellular processes including apoptosis, proliferation, and differentiation. It has a modular domain architecture consisting of an Src homology 2 domain (SH2) followed by two Src homology 3 (SH3) domains. The structures and ligand-binding properties of the SH2 and the middle SH3 domains are well-characterized. Several studies suggest that the C-terminal SH3 domain plays an important regulatory role in the protein; however, no structural information is available on this domain, and relatively little is known about its binding partners. In the current work, we have solved the solution NMR structure of the C-terminal SH3 domain. The domain adopts the standard SH3 fold comprising a five-stranded beta barrel. In agreement with alignment and modeling studies, the structure indicates that the canonical-binding surface of the SH3 domain is unusually polar and suggests that this domain may not bind typical PXXP ligands or that it may bind them with reduced affinity. Thermodynamic and kinetic studies show that the domain folds in a reversible two-state manner and that the stability of the fold is similar to that observed for other SH3 domains. These studies offer some insight into the likely structural and thermodynamic consequences of point mutations in the cSH3 domain that are known to deregulate Crk-II function. Our results set the stage for a better understanding the role of the cSH3 domain in the context of the full-length protein.
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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.