Martin E. M. Noble

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This review will focus on the role of the activation segment in the mediation of these different aspects of and David J. Owen control. The activation segment is defined as the region Laboratory of Molecular Biophysics spanning conserved sequences DFG and APE and cor-and Oxford Centre for Molecular Sciences responds to residues 184–208 in cAPK (Taylor and(More)
The alpha subunit of the endocytotic AP2 adaptor complex contains a 30 kDa "appendage" domain, which is joined to the rest of the protein via a flexible linker. The 1.9 A resolution crystal structure of this domain reveals a single binding site for its ligands, which include amphiphysin, Eps15, and epsin. This domain when overexpressed in COS7 fibroblasts(More)
at the plasma membrane, AP2, was shown to bind and cluster transmembrane proteins destined for internaliza-tion and to promote clathrin polymerization. The formation of a cage structure from clathrin helps to invaginate the membrane, and the scission of the nascent vesicle is achieved with the aid of the GTPase dynamin (Schmid Hills Road et al., 1998). This(More)
CDK9, the kinase of positive transcription elongation factor b (P-TEFb), stimulates transcription elongation by phosphorylating RNA polymerase II and transcription elongation factors. Using kinetic analysis of a human P-TEFb complex consisting of CDK9 and cyclin T, we show that the CDK9 C-terminal tail sequence is important for the catalytic mechanism and(More)
The refined crystal structures of chicken, yeast and trypanosomal triosephosphate isomerase (TIM) have been compared. TIM is known to exist in an "open" (unliganded) and "closed" (liganded) conformation. For chicken TIM only the refined open structure is available, whereas for yeast TIM and trypanosomal TIM refined structures of both the open and the closed(More)
Figure S1. Sequence Alignment of α−Parvin-CH C with Homologous Type-1 CH domains Secondary structural elements and the characteristic C/E-loop insertion and N-linker helix of α-parvin are indicated. Regions forming the LD binding site are labelled in green. Grey boxes denote the actin binding sites ABS1 and ABS2, which are conserved across type-1 CH(More)
The ubiquitin-proteasome system targets selected proteins for degradation by the 26S proteasome. Rpn12 is an essential component of the 19S regulatory particle and plays a role in recruiting the extrinsic ubiquitin receptor Rpn10. In the present paper we report the crystal structure of Rpn12, a proteasomal PCI-domain-containing protein. The structure helps(More)
CDK1 is the only essential cell cycle CDK in human cells and is required for successful completion of M-phase. It is the founding member of the CDK family and is conserved across all eukaryotes. Here we report the crystal structures of complexes of CDK1-Cks1 and CDK1-cyclin B-Cks2. These structures confirm the conserved nature of the inactive monomeric CDK(More)
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