Modular binding domains in signal transduction proteins

Article Abstract:

The SH2, PH and SH3 binding domains are true protein domains that exhibit binding specificity. They are compact units with isolated structures, each with an N- and a C-terminal positioned against each other. They occur in a variety of signal transduction proteins such as protein phosphatases, protein kinases, phospholipases and transcription factors. All eukaryotic organisms contain PH and SH3 domains, but SH2 domains are absent in yeast. The binding potential of these domains to a specific phosphoprotein varies with local protein levels.

Analysis, Proteins, Binding sites (Biochemistry), Active sites (Biochemistry), Protein structure, Cooperative binding (Biochemistry)

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A putative modular domain present in diverse signaling proteins

Article Abstract:

The identification of a putative modular domain present in various signaling proteins is reported. The modular domain was observed to be present in 3BP2, an Src homology 3-binding proteins (SH3-binding proteins). It is a 100-amino acid protein with sequence similarity to several other proteins, indicating a role in mediating protein associations. Since it was first identified in the platelet protein pleckstrin, the proposed name for the putative modular domain is pleckstrin homology, or PH, domain.

Letter to the Editor

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Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems

Article Abstract:

The experiments relating to dynamic cellular behavior are discussed. Current and future areas in interest in cell signaling are detailed.

Science & research

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