ArticleThe EMBO journal2001
Novel recognition mode between Vav and Grb2 SH3 domains.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
37 citing papers in PubMed, 113 citations in OpenAlex.
- Spatially resolved in silico modeling of NKG2D signaling kinetics suggests a key role of NKG2D and Vav1 Co-clustering in generating natural killer cell activation.PLoS computational biology · 2022Article
- Negative times negative equals positive, THEMIS sets the rule on thymic selection and peripheral T cell responses.Biomedical journal · 2022Review
- A dynamical view of protein-protein complexes: Studies by molecular dynamics simulations.Frontiers in molecular biosciences · 2022Article
- Experimental Characterization of the Interaction between the N-Terminal SH3 Domain of Crkl and C3G.International journal of molecular sciences · 2021Article
- Conserved patterns and interactions in the unfolding transition state across SH3 domain structural homologues.Protein science : a publication of the Protein Society · 2021Article
- CoRNeA: A Pipeline to Decrypt the Inter-Protein Interfaces from Amino Acid Sequence Information.Biomolecules · 2020Article
- Single residue in CD28-costimulated CAR-T cells limits long-term persistence and antitumor durability.The Journal of clinical investigation · 2020Article
- A Quantitative Tri-fluorescent Yeast Two-hybrid System: From Flow Cytometry toMolecular & cellular proteomics : MCP · 2020Article
- High-Affinity Interactions of the nSH3/cSH3 Domains of Grb2 with the C-Terminal Proline-Rich Domain of SOS1.Journal of the American Chemical Society · 2020Article
- Review
- Identification of two distinct peptide-binding pockets in the SH3 domain of human mixed-lineage kinase 3.The Journal of biological chemistry · 2018Article
- Article
- A Novel Vav3 Homolog Identified in Lamprey, Lampetra japonica, with Roles in Lipopolysaccharide-Mediated Immune Response.International journal of molecular sciences · 2017Article
- Grb2 carboxyl-terminal SH3 domain can bivalently associate with two ligands, in an SH3 dependent manner.Scientific reports · 2017Article
- A Machine Learning Approach for Hot-Spot Detection at Protein-Protein Interfaces.International journal of molecular sciences · 2016Article
- Vav family exchange factors: an integrated regulatory and functional view.Small GTPases · 2014Review
- SH3 domains: modules of protein-protein interactions.Biophysical reviews · 2013Review
- Article
- Mechanism and function of Vav1 localisation in TCR signalling.Journal of cell science · 2012Article
- Studies of novel interactions between Nck and VAV SH3 domains.Communicative & integrative biology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vav is a guanine nucleotide exchange factor for the Rho/Rac family that is expressed exclusively in hematopoietic cells. Growth factor receptor-bound protein 2 (Grb2) has been proposed to play important roles in the membrane localization and activation of Vav through dimerization of its C-terminal Src-homology 3 (SH3) domain (GrbS) and the N-terminal SH3 domain of Vav (VavS). The crystal structure of VavS complexed with GrbS has been solved. VavS is distinct from other SH3 domain proteins in that its binding site for proline-rich peptides is blocked by its own RT loop. One of the ends of the VavS beta-barrel forms a concave hydrophobic surface. The GrbS components make a contiguous complementary interface with the VavS surface. The binding site of GrbS for VavS partially overlaps with the canonical binding site for proline-rich peptides, but is definitely different. Mutations at the interface caused a decrease in the binding affinity of VavS for GrbS by 4- to 40-fold. The structure reveals how GrbS discriminates VavS specifically from other signaling molecules without binding to the proline-rich motif.
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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.