We are analyzing https://link.springer.com/article/10.1186/1478-811x-10-32.

Title:
Phosphotyrosine recognition domains: the typical, the atypical and the versatile | Cell Communication and Signaling
Description:
SH2 domains are long known prominent players in the field of phosphotyrosine recognition within signaling protein networks. However, over the years they have been joined by an increasing number of other protein domain families that can, at least with some of their members, also recognise pTyr residues in a sequence-specific context. This superfamily of pTyr recognition modules, which includes substantial fractions of the PTB domains, as well as much smaller, or even single member fractions like the HYB domain, the PKCδ and PKCθ C2 domains and RKIP, represents a fascinating, medically relevant and hence intensely studied part of the cellular signaling architecture of metazoans. Protein tyrosine phosphorylation clearly serves a plethora of functions and pTyr recognition domains are used in a similarly wide range of interaction modes, which encompass, for example, partner protein switching, tandem recognition functionalities and the interaction with catalytically active protein domains. If looked upon closely enough, virtually no pTyr recognition and regulation event is an exact mirror image of another one in the same cell. Thus, the more we learn about the biology and ultrastructural details of pTyr recognition domains, the more does it become apparent that nature cleverly combines and varies a few basic principles to generate a sheer endless number of sophisticated and highly effective recognition/regulation events that are, under normal conditions, elegantly orchestrated in time and space. This knowledge is also valuable when exploring pTyr reader domains as diagnostic tools, drug targets or therapeutic reagents to combat human diseases.
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Keywords {🔍}

pubmed, domain, google, scholar, cas, domains, binding, protein, cell, tyrosine, kinase, central, ptyr, ptb, proteins, biol, figure, peptide, phosphorylation, signalling, structure, recognition, cancer, interaction, human, signaling, phosphotyrosine, residues, ligand, mol, site, specificity, motif, receptor, binds, activity, sequence, pocket, nature, phosphorylated, src, structural, pawson, kinases, sci, phosphatase, interactions, identified, tensin, substrate,

Topics {✒️}

arp2/3-complex-dependent actin-based motility shawn sc li g-protein beta-gamma subunits phosphorylation-dependent partner switching ptyr-mediated host-pathogen interactions wd40/beta-transducin repeat serine/threonine-protein kinase wnk1 full size image post-translational modifications high-affinity phosphotyrosine-independent interaction interpreting genotype-phenotype relationships clathrin-coated vesicle budding t-cell receptor subunit phospho-modification information n-wasp exchange limits ser/thr kinase displaying including immune-related disorders beta-adrenergic receptor kinase proline-driven conformational switch dna-tagged sh2 domains raf-1-mediated activated phosphorylation breast cancer therapeutics phospho-tyrosine signaling machinery partner protein switching erbb-receptor kinase family tri-phosphorylated raf-1 peptide regulate sh2-ligand interactions fourth position c-terminal n-terminal residues forming dual-specificity phosphatase subfamily cancer-causing mutations tend regulated protein-protein interactions tyrosine phosphorylation-dependent manner engages residues c-terminal x-chromosome-linked agammaglobulinemia phosphotyrosine-dependent sh2 interaction bcr-abl inhibits leukemogenesis protein-based agent called domain-based probe technology anti-parallel β-strands article download pdf phosphotyrosine-independent sequence recognition small-molecule drug discovery c-terminal sh2 domain yield protein-based reagents anti-parallel β-strand e3 ligase c-cbl dynamic view pleckstrin homology-phosphotyrosine binding pseudophosphatase mk-styx interacts

Questions {❓}

Cozzone AJ: Bacterial tyrosine kinases: novel targets for antibacterial therapy?
So does nature have more domain members capable of pTyr-epitope binding that remain to be identified?
The Spt6 SH2 domain: a common ancestor of pTyr recognition?

Schema {🗺️}

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         description:SH2 domains are long known prominent players in the field of phosphotyrosine recognition within signaling protein networks. However, over the years they have been joined by an increasing number of other protein domain families that can, at least with some of their members, also recognise pTyr residues in a sequence-specific context. This superfamily of pTyr recognition modules, which includes substantial fractions of the PTB domains, as well as much smaller, or even single member fractions like the HYB domain, the PKCδ and PKCθ C2 domains and RKIP, represents a fascinating, medically relevant and hence intensely studied part of the cellular signaling architecture of metazoans. Protein tyrosine phosphorylation clearly serves a plethora of functions and pTyr recognition domains are used in a similarly wide range of interaction modes, which encompass, for example, partner protein switching, tandem recognition functionalities and the interaction with catalytically active protein domains. If looked upon closely enough, virtually no pTyr recognition and regulation event is an exact mirror image of another one in the same cell. Thus, the more we learn about the biology and ultrastructural details of pTyr recognition domains, the more does it become apparent that nature cleverly combines and varies a few basic principles to generate a sheer endless number of sophisticated and highly effective recognition/regulation events that are, under normal conditions, elegantly orchestrated in time and space. This knowledge is also valuable when exploring pTyr reader domains as diagnostic tools, drug targets or therapeutic reagents to combat human diseases.
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         Signaling circuit
         Cell Biology
         Protein-Ligand Interactions
         Receptors
         Cytokines and Growth Factors
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      name:Biological Systems Architecture Group, Weatherall Institute of Molecular Medicine, Department of Oncology, University of Oxford, John Radcliffe Hospital, Oxford, UK
      name:Department of Biochemistry and the Siebens-Drake Medical Research Institute, Schulich School of Medicine and Dentistry, University of Western Ontario, London, Canada

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