Crystal structure of the Dbl and Pleckstrin homology domains from the Human Son of Sevenless protein

Article Abstract:

Proteins with Dbl homology (DH) domains operate as specific guanine nucleotide exchange factors, activating Rho-family GTPases. All DH domains have C-terminal pleckstrin homology (PH) domains that may be involved in targeting and regulatory functions. The crystal structure of a fragment of human Son of sevenless protein having the DH and PH domains, was determined at 2.3 A resolution. The active DH domain site is close to the interface between the DH and PH domains.

Observations, Proteins, Rho(D) immune globulin

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High resolution crystal structure of a paired (Pax) class cooperative homeodomain dimer on DNA

Article Abstract:

Comparison of the 2.0 angstrom resolution crystal structure of the paired (Pax) class homeodomain dimer bound to DNA with the homeodomains bound monomerically to DNA shows that the binding of a paired homeodomain to one of the TAAT sequences in a palindromic target site leads to the formation of a template for the cooperative reaction with another homeodomain. This allows the identification of target sequences that are adequate for ensuring specificity.

DNA, Protein binding

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A myristoyl/phosphotyrosine switch regulates c-Abl

Article Abstract:

Structure-function studies reveal a myristoyl/phosphotyrosine switch in c-Abl tyrosine kinase, which is involved in the regulation of docking and acessing the SH2 domain leading to cellular activation of c-Abl by tyrosine-phosphorylated proteins and its intracellular mobility. Results throw light on the mechanism of action of the anti-cancer drug STI-571.

United States, Germany, Pharmaceutical Preparation Manufacturing, Pharmaceutical preparations, Anticancer Drugs, Chemotherapeutic Drugs, Anticancer Immunostimulant Preps, Physiological aspects, Antineoplastic agents, Protein kinases, Structure-activity relationships (Biochemistry), Enzyme regulation, Structure, Antimitotic agents

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