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PhosphoSerine/threonine binding domains: you can't pSERious?
Yaffe, M B; Smerdon, S J.
Afiliación
  • Yaffe MB; Center for Cancer Research, Massachusetts Institute of Technology, 77 Massachusetts Avenue, E18-580, Cambridge, MA 02139, USA. myaffe@mit.edu
Structure ; 9(3): R33-8, 2001 Mar 07.
Article en En | MEDLINE | ID: mdl-11286893
ABSTRACT
The fundamental biological importance of protein phosphorylation is underlined by the existence of more than 500 protein kinase genes within the human genome. In many cases, phosphorylation on serine, threonine, and tyrosine residues creates binding surfaces for a variety of phospho-amino acid binding proteins/modules. Here, we review the insights into serine/threonine phosphorylation-dependent signal transduction processes provided by structures of several of these proteins and their complexes.
Asunto(s)
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fosfoserina / Fosfotreonina Límite: Animals / Humans Idioma: En Revista: Structure Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA / BIOTECNOLOGIA Año: 2001 Tipo del documento: Article País de afiliación: Estados Unidos
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fosfoserina / Fosfotreonina Límite: Animals / Humans Idioma: En Revista: Structure Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA / BIOTECNOLOGIA Año: 2001 Tipo del documento: Article País de afiliación: Estados Unidos