Crystal structure of the pleckstrin homology domain from dynamin (original) (raw)
References
Mayer, B.J., Ren, B.J., Clark, K.L. & Baltimore, D. A putative modular domain present in diverse signaling proteins. Cell73, 629–630(1993). ArticleCASPubMed Google Scholar
Musacchio, A., Gibson, T., Rise, P., Thompson, J. & Saraste, M. The PH domain - a common piece in the structural patchwork of signaling proteins. Trends biochem. Sci., 343–348 (1993).
Shaw, G. Identification of novel pleckstrin homology (PH) domains provides a hypothesis for PH domain function. Biochem. biophys. Res. Commun.195, 1145–1151 (1993). ArticleCASPubMed Google Scholar
Koch, W.J., Inglese, J., Stone, W.C. & Lefkowitz, R.J. The binding site for the β,γ-subunits of heterotrimetic G-proteins on the β-adrenergic-receptor kinase. J. biol. Chem.268, 8256–8260 (1993). CASPubMed Google Scholar
Touhara, K., Inglese, J., Pitcher, J.A., Shaw, G. & Lefkowitz, R.J. Binding of G-protein β,γ-subunits to pleckstrin homology domains. J. biol. Chem.269, 10217–10220 (1993). Google Scholar
Davis, L.H. & Bennett, V. Identification of 2 regions of β-spectrin that bind to distinct sites in brain membranes. J. biol. Chem.269, 4409–4416 (1994). CASPubMed Google Scholar
Yoon, H.S., Hajduk, P.J., Petros, A.M., Olejniczak, E.T., Meadows, R.P. & Fesik, S.W. Solution structure of a pleckstrin-homology domain. Nature369, 672–675 (1994). ArticleCASPubMed Google Scholar
Macias, M.J., Musacchio, A., Ponstingl, H., Nilges, M., Saraste, M. & Oschkinat, H. Structure of the pleckstrin homology domain from β- spectrin. Nature369, 675–677 (1994). ArticleCASPubMed Google Scholar
van der Bliek, A.M., Redelmeier, T.E., Damke, H., Tisdale, E.J., Meyerowitz, E.M. & Schmid, S.L. Mutations in human dynamin block an intermediate stage in coated vesicle formation. J. cell Biol.122, 553–563 (1993). ArticleCASPubMed Google Scholar
Herskovits, J.S., Burgess, C.C., Obar, R.A. & Vallee, R.B., Effects of mutant rat dynamin on endocytosis. J. cell Biol.122, 565–578 (1993). ArticleCASPubMed Google Scholar
Shpetner, H.S. & Valle, R.B. Dynamin is a GTPase stimulated to high levels of activity by microtubules. Nature355, 733–735 (1992). ArticleCASPubMed Google Scholar
Ando, A. et al. A complex of Grb2 dynamin binds to tyrosine phosphorylated insulin-receptor substrate-after insulin-treatment. EMBO J.13, 3033–3038 (1994). ArticleCASPubMedPubMed Central Google Scholar
Gout, I. et al. The GTPase dynamin binds to and is activated by a subset of SH3 domains. Cell75, 25–36 (1993). ArticleCASPubMed Google Scholar
Thomas, I.D., Sideras, P., Smith, C.I.E., Vorechovsky, I., Chapman, V. & Paul, W.E. Colocalization of X-linked agammaglobulinemia and X-linked immunodeficiency genes. Science261, 355–358 (1993). ArticleCASPubMed Google Scholar
Rawlings, D.I. et al. Mutation of a unique region of Brutons tyrosine kinase in immunodeficient xid mice. Science261, 358–361 (1993). ArticleCASPubMed Google Scholar
Blundell, T.L. & Johnson, L.N. in Protein crystallography (Academic, London; 1976). Google Scholar
Cowan, S.W., Newcomer, M.E. & Jones, T.A. Crystallographic refinement of human serum retinol binding-protein at 2Å resolution. Proteins.8, 44–61 (1990). ArticleCASPubMed Google Scholar
Sali, A. & Blundell, T.L. The definition of topological equivalence in homologous and analogous structures: a procedure involving a comparison of local properties and relationships. J. molec. Biol.212, 403–442 (1990). ArticleCASPubMed Google Scholar
Pawson, T. & Schlessinger, J. SH2 and SH3 domains. Current Biol.3, 434–441 (1993). ArticleCAS Google Scholar
Simonds, W.F., Manji, H.K., Garritsen, A., Lupas, A.N. G-proteins and bark - a new twist for the coiled-coil. Trends biochem. Sci.18, 315–317 (1993). ArticleCASPubMed Google Scholar
Ellis, M.V., Carne, A. & Katan, M. Structural requirements of phosphatidylinositol-specific phospholipase-cδ for enzyme activity. Eur J. Biochem.213, 339–347 (1993). ArticleCASPubMed Google Scholar
Leslie, A.G.W. in Crystallographic Computing (Oxford Univ. Press; 1990).
Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta crystallogr.A47, 110–119 (1991). ArticleCAS Google Scholar
Driessen, H., Haneef, M.I.J., Harris, G.W., Howlin, B., Khan, G. & Moss, D.S. Restrain: restrained structure-factor least-squares refinement program for macromolecular structures. J. appl. Crystallogr.22, 510–516 (1989). ArticleCAS Google Scholar
Brunger, A.T. X-PLOR Version 3.1 Manual (Yale Univ. Press, New Haven; 1992). Google Scholar
Evans, S.V. SETOR: hardware-lighted three-dimensional solid model representations of marcomolecules. J. molec. Graphics11, 134–138 (1993). ArticleCAS Google Scholar
Hutchinson, E.G. & Thornton, J.M. Hera - a program to draw schematic diagrams of protein secondary structures. Proteins8, 203–212 (1990). ArticleCASPubMed Google Scholar
Kabsch, W. & Sander, C. Dictionary of protein secondary structure. Pattern recognition of hydrogen bonded and geometrical features. Biopolymers22, 2577–2637 (1983). ArticleCASPubMed Google Scholar
Overington, J.R., Johnson, M.S., Sali, A. & BIundell, T.L. Tertiary structural constraints on protein evolutionary diversity: templates, key residues and structure prediction. Proc. Royal Soc.B241, 132–145 (1990). Google Scholar