D Cowburn

Summary

Affiliation: The Rockefeller University
Country: USA

Publications

  1. ncbi request reprint Peptide recognition by PTB and PDZ domains
    D Cowburn
    Rockefeller University, New York, NY 10021 6399, USA
    Curr Opin Struct Biol 7:835-8. 1997
  2. ncbi request reprint Adaptors and integrators
    D Cowburn
    The Rockefeller University, 1230 York Avenue, New York, NY 10021 6399, USA
    Structure 4:1005-8. 1996
  3. ncbi request reprint Rescuing a destabilized protein fold through backbone cyclization
    J A Camarero
    The Laboratory of Synthetic Protein Chemistry, New York, NY 10021, USA
    J Mol Biol 308:1045-62. 2001
  4. ncbi request reprint The solution structure and dynamics of the pleckstrin homology domain of G protein-coupled receptor kinase 2 (beta-adrenergic receptor kinase 1). A binding partner of Gbetagamma subunits
    D Fushman
    Laboratory of Physical Biochemistry, The Rockefeller University, New York, New York 10021 6399, USA
    J Biol Chem 273:2835-43. 1998
  5. ncbi request reprint A novel, specific interaction involving the Csk SH3 domain and its natural ligand
    R Ghose
    The Rockefeller University, 1230 York Avenue, New York, New York 10021 6399, USA
    Nat Struct Biol 8:998-1004. 2001
  6. ncbi request reprint Simulated and NMR-derived backbone dynamics of a protein with significant flexibility: a comparison of spectral densities for the betaARK1 PH domain
    S Pfeiffer
    The Rockefeller University, 1230 York Avenue, New York, NY 10021-6399, USA
    J Am Chem Soc 123:3021-36. 2001
  7. ncbi request reprint Novel mechanism of regulation of the non-receptor protein tyrosine kinase Csk: insights from NMR mapping studies and site-directed mutagenesis
    A Shekhtman
    The Rockefeller University, 1230 York Ave, New York, NY 10021 6399, USA
    J Mol Biol 314:129-38. 2001
  8. ncbi request reprint Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists
    J M McDonnell
    Rockefeller University, New York, New York 10021, USA
    Cell 96:625-34. 1999
  9. ncbi request reprint The solution structure of the pleckstrin homology domain of human SOS1. A possible structural role for the sequential association of diffuse B cell lymphoma and pleckstrin homology domains
    J Zheng
    The Rockefeller University, New York, New York 10021, USA
    J Biol Chem 272:30340-4. 1997
  10. ncbi request reprint Determination of the rotational diffusion tensor of macromolecules in solution from nmr relaxation data with a combination of exact and approximate methods--application to the determination of interdomain orientation in multidomain proteins
    R Ghose
    Rockefeller University, 1230 York Avenue, New York, New York 10021, USA
    J Magn Reson 149:204-17. 2001

Detail Information

Publications22

  1. ncbi request reprint Peptide recognition by PTB and PDZ domains
    D Cowburn
    Rockefeller University, New York, NY 10021 6399, USA
    Curr Opin Struct Biol 7:835-8. 1997
    ..For both PTB and PDZ classes, functional activities are still not fully defined: it is possible that these domain classes, along with pleckstrin homology domains, have multiple roles...
  2. ncbi request reprint Adaptors and integrators
    D Cowburn
    The Rockefeller University, 1230 York Avenue, New York, NY 10021 6399, USA
    Structure 4:1005-8. 1996
    ..The PTB domain expands both the PH-domain set and peptide-protein recognition motifs; the PDZ domain shows an intriguing resemblance...
  3. ncbi request reprint Rescuing a destabilized protein fold through backbone cyclization
    J A Camarero
    The Laboratory of Synthetic Protein Chemistry, New York, NY 10021, USA
    J Mol Biol 308:1045-62. 2001
    ..The ability to rescue the destabilized mutant indicates that circularization may be a useful tool in protein engineering programs geared towards generating minimized proteins...
  4. ncbi request reprint The solution structure and dynamics of the pleckstrin homology domain of G protein-coupled receptor kinase 2 (beta-adrenergic receptor kinase 1). A binding partner of Gbetagamma subunits
    D Fushman
    Laboratory of Physical Biochemistry, The Rockefeller University, New York, New York 10021 6399, USA
    J Biol Chem 273:2835-43. 1998
    ..This suggests that the C-terminal segment of the PH domain may function to mediate protein-protein interactions with the targets of PH domains...
  5. ncbi request reprint A novel, specific interaction involving the Csk SH3 domain and its natural ligand
    R Ghose
    The Rockefeller University, 1230 York Avenue, New York, New York 10021 6399, USA
    Nat Struct Biol 8:998-1004. 2001
    ..NMR relaxation analysis suggests that Csk-SH3 has different dynamic properties in the various subsites important for peptide recognition...
  6. ncbi request reprint Simulated and NMR-derived backbone dynamics of a protein with significant flexibility: a comparison of spectral densities for the betaARK1 PH domain
    S Pfeiffer
    The Rockefeller University, 1230 York Avenue, New York, NY 10021-6399, USA
    J Am Chem Soc 123:3021-36. 2001
    ..The analysis of spectral densities provides additional information regarding the comparison of the simulated and experimental data, not available from the model-free analysis...
  7. ncbi request reprint Novel mechanism of regulation of the non-receptor protein tyrosine kinase Csk: insights from NMR mapping studies and site-directed mutagenesis
    A Shekhtman
    The Rockefeller University, 1230 York Ave, New York, NY 10021 6399, USA
    J Mol Biol 314:129-38. 2001
    ..We conclude that the SH3-SH2 linker plays a major role in the activation of the Csk catalytic domain...
  8. ncbi request reprint Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists
    J M McDonnell
    Rockefeller University, New York, New York 10021, USA
    Cell 96:625-34. 1999
    ..BID's activity is regulated by a Caspase 8-mediated cleavage event, exposing the BH3 domain and significantly changing the surface charge and hydrophobicity, resulting in a change of cellular localization...
  9. ncbi request reprint The solution structure of the pleckstrin homology domain of human SOS1. A possible structural role for the sequential association of diffuse B cell lymphoma and pleckstrin homology domains
    J Zheng
    The Rockefeller University, New York, New York 10021, USA
    J Biol Chem 272:30340-4. 1997
    ....
  10. ncbi request reprint Determination of the rotational diffusion tensor of macromolecules in solution from nmr relaxation data with a combination of exact and approximate methods--application to the determination of interdomain orientation in multidomain proteins
    R Ghose
    Rockefeller University, 1230 York Avenue, New York, New York 10021, USA
    J Magn Reson 149:204-17. 2001
    ..This approach is then used to estimate the relative orientation of SH3 and SH2 domains in the SH(32) dual-domain construct of Abelson kinase complexed with a consolidated ligand...
  11. ncbi request reprint Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk
    X Wu
    Rockefeller University, New York, NY 10021, USA
    Structure 3:215-26. 1995
    ..The presence of a lysine instead of an arginine in the peptides derived from C3G appears to be crucial for this specificity towards c-Crk...
  12. ncbi request reprint The structure of the IgE Cepsilon2 domain and its role in stabilizing the complex with its high-affinity receptor FcepsilonRIalpha
    J M McDonnell
    The Rockefeller University, New York, New York 10021-6399, USA
    Nat Struct Biol 8:437-41. 2001
    ..These interactions of Cepsilon2 with both FcepsilonRIalpha and Cepsilon3-4 provide a structural explanation for the exceptionally slow dissociation of the IgE-FcepsilonRIalpha complex...
  13. ncbi request reprint The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct
    Y Q Gosser
    Rockefeller University, New York, NY 10021, USA
    Structure 3:1075-86. 1995
    ..We expect that the solution structures of Abl SH3, Abl SH2 and Abl SH(32) (a dual domain comprising SH3 and SH2 subdomains) will contribute to a structural basis for understanding the mechanism of the Abl 'regulatory apparatus'...
  14. ncbi request reprint Enhanced affinities and specificities of consolidated ligands for the Src homology (SH) 3 and SH2 domains of Abelson protein-tyrosine kinase
    D Cowburn
    Rockefeller University, New York, New York 10021, USA
    J Biol Chem 270:26738-41. 1995
    ..These results suggest that consolidated ligands may be generally useful reagents for probing structural and functional activities of multidomain proteins...
  15. ncbi request reprint Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions
    K Shuai
    Laboratory of Molecular Cell Biology, Rockefeller University, New York, New York 10021
    Cell 76:821-8. 1994
    ..Dimerization involving SH2 recognition of specific phosphotyrosyl peptides may well provide a prototype for interactions among family members of STAT proteins to form different transcription complexes...
  16. ncbi request reprint Peptide chemical ligation inside living cells: in vivo generation of a circular protein domain
    J A Camarero
    Laboratory of Synthetic Protein Chemistry, The Rockefeller University, New York, NY 10021, USA
    Bioorg Med Chem 9:2479-84. 2001
    ..This work represents an important step towards the in vivo generation of small backbone cyclic peptides for use in basic biological research...
  17. ncbi request reprint Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms
    G Waksman
    Rockefeller University, New York, New York 10021
    Cell 72:779-90. 1993
    ..The crystal structure of Src SH2 in the absence of peptide has been determined at 2.5 A resolution, and comparison with the structure of the high affinity complex reveals only localized and relatively small changes...
  18. ncbi request reprint Modular peptide recognition domains in eukaryotic signaling
    J Kuriyan
    Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021, USA
    Annu Rev Biophys Biomol Struct 26:259-88. 1997
    ..In addition, the mechanism of cooperative interactions between these domains is discussed...
  19. pmc A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein
    C H Lee
    Laboratory of Molecular Biophysics, Rockefeller University, New York, NY 10021, USA
    EMBO J 14:5006-15. 1995
    ..The binding of a peptide containing the Nef PxxP motif showed > 300-fold weaker affinity for Hck SH3 than full-length Nef...
  20. pmc Accurate quantitation of protein expression and site-specific phosphorylation
    Y Oda
    The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA
    Proc Natl Acad Sci U S A 96:6591-6. 1999
    ....
  21. ncbi request reprint Three-dimensional solution structure of the src homology 2 domain of c-abl
    M Overduin
    Laboratories of The Rockefeller University New York, New York 10021
    Cell 70:697-704. 1992
    ..Comparison with other SH2 sequences supports a common global fold and mode of phosphotyrosine binding for this family...
  22. pmc Secondary structure of Src homology 2 domain of c-Abl by heteronuclear NMR spectroscopy in solution
    M Overduin
    Laboratories of the Rockefeller University, New York, NY 10021
    Proc Natl Acad Sci U S A 89:11673-7. 1992
    ..Residues believed to be involved in phosphotyrosyl ligand binding are on a face of one beta-sheet. The alignment of homologous sequences on the basis of secondary structure suggests a conserved global fold in a family of SH2 domains...