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Interaction of a G-protein β-subunit with a conserved sequence in Ste20/PAK family protein kinases
A binding site for the G-protein β-subunit (Gβ) in the non-catalytic carboxy-terminal regions of Ste20 and its mammalian homologues, the p21-activated protein kinases (PAKs) is identified, providing a possible model for a role of these kinases in Gβγ-mediated signal transduction in organisms ranging from yeast to mammals.
The Structure of calnexin, an ER chaperone involved in quality control of protein folding.
Crystal structure of the bb' domains of the protein disulfide isomerase ERp57.
The alpha/beta hydrolase fold.
There are now four groups of enzymes which contain catalytic triads and which are related by convergent evolution towards a stable, useful active site: the eukaryotic serine proteases, the cysteine protease, subtilisins and the alpha/beta hydrolase fold enzymes.
Relationship between sequence conservation and three‐dimensional structure in a large family of esterases, lipases, and related proteins
- M. Cygler, J. Schrag, B. P. Doctor
- BiologyProtein science : a publication of the Protein…
- 1 March 1993
An improved alignment of a collection of 32 related amino acid sequences of other esterases, lipases, and related proteins was obtained, and 24 residues are found to be invariant in 29 sequences of hydrolytic enzymes, and an additional 49 are well conserved.
Insights into interfacial activation from an open structure of Candida rugosa lipase.
The structure of the Candida rugosa lipase determined at 2.06-A resolution reveals a conformation with a solvent-accessible active site and provides a new image of the substrate binding region and active site access, which is different from that inferred from theructure of the "closed" form of the G. candidum lipase.
Two conformational states of Candida rugosa lipase
- P. Grochulski, Yunge Li, J. Schrag, M. Cygler
- Chemistry, BiologyProtein science : a publication of the Protein…
- 1 January 1994
Comparison of this structure with the previously determined “open” form of this lipase, in which the active site is accessible to the solvent and presumably the substrate, shows that the transition between these 2 states requires only movement of the flap.
Three-dimensional structure of the HSV1 nucleocapsid
Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism.
The observed interactions between the aldimine and the side chains in the substrate binding site explain the specificity for the substrate and provide the basis for a detailed proposal of the reaction mechanism of KBL.