Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor

Article Abstract:

The structure of the insulin receptor substrate-1 phosphotyrosine-binding (PTB) domain has been established independently and in a form bound to the juxtamembrane region of the insulin receptor. The PTB site is a seven-stranded beta sandwich capped by a C-terminal helix. The insulin receptor phosphopeptide is present in an L-shaped cleft on PTB. The peptide's N-terminal amino acids form an extra strand in the beta sandwich. These interactions are involved in the recognition of phosphorylated NPXY sequence motifs by PTB.

Structure-activity relationships (Biochemistry), Binding sites (Biochemistry), Active sites (Biochemistry), Insulin, Insulin receptors

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Crystal structures of a Formin Homology-2 domain reveal tethered dimer architecture

Article Abstract:

The defining feature of Formins is a highly conserved approximately 400-residue region in which the Formin Homology-2 (FH2) domain has recently been found to nucleate actin filaments. The mostly alpha helical FH2 domain in which two elongated actin binding heads are tied together at either end by an unusual laaso and linker structure forms a unique 'tethered dimer'.

Homology (Biology)

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Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis

Article Abstract:

The demonstration of FH1-FH2 domain acceleration hydrolysis of ATP coupled to profilin-actin polymerization is presented that uses the derived free energy for processive polymerization increasing 15-fold the rate constant for profillin-actin association to barbed ends. Profillin is required for and takes part in the processive function.

Methods, Hydrolysis, Adenosine triphosphatase genes, ATP genes

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