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Mechanism of Activation of the RAF-ERK Signaling Pathway by Oncogenic Mutations of B-RAF
Structure of the mitotic checkpoint complex
This study shows how APC/C inhibition is coupled to degron recognition by co-activators and how p31comet disrupts MCC assembly to antagonize the SAC.
The Crystal Structure of Human Eukaryotic Release Factor eRF1—Mechanism of Stop Codon Recognition and Peptidyl-tRNA Hydrolysis
Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution.
The model presents a framework for understanding not only the classical Mn2+/Mg2+‐dependent protein phosphatases but also the sequence‐related domains of mitochondrial pyruvate dehydrogenase phosphatase, the Bacillus subtilusosphatase SpoIIE and a 300‐residue domain within yeast adenyl cyclase.
The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR‐mediated protein–protein interactions
The crystal structure of the TPR domain of a protein phosphatase, PP5, is reported, which indicates that multiple‐TPR motif proteins would fold into a right‐handed super‐helical structure with a continuous helical groove suitable for the recognition of target proteins, hence defining a novel mechanism for protein recognition.
Wild-type and mutant B-RAF activate C-RAF through distinct mechanisms involving heterodimerization.
Crystal structure of an activated Akt/Protein Kinase B ternary complex with GSK3-peptide and AMP-PNP
- Jing Yang, P. Cron, V. Good, Vivienne Thompson, B. Hemmings, D. Barford
- Biology, ChemistryNature Structural Biology
- 1 December 2002
The crystal structures of activated kinase domains of PKB in complex with a GSK3β-peptide substrate and an ATP analog explain how PKB selects for protein substrates distinct from those of PKA.
Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation.
Molecular discrimination of structurally equivalent Lys 63‐linked and linear polyubiquitin chains
- D. Komander, Francisca E. Reyes-Turcu, J. Licchesi, P. Odenwaelder, K. Wilkinson, D. Barford
- BiologyEMBO reports
- 1 May 2009
Crystallized Lys 63‐linked and linear ubiquitin dimers are revealed, revealing that both adopt equivalent open conformations, forming no contacts between Ubiquitin molecules and thereby differing significantly from Lys 48‐linked ubiquitIn chains.
Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
It is proposed that this unusual protein modification both protects the active-site cysteine residue of PTP1B from irreversible oxidation to sulphonic acid and permits redox regulation of the enzyme by promoting its reversible reduction by thiols.