… pVHL is the substrate recognition component of this complex and … The C4 hydroxyproline
residue in HIF-1α (HyP564) is almost … structure of pVHL in complex with a hydroxylated HIF-1α …

… The original linear motif described to be critical for pVHL/HIF-1α recognition was the LxxLAP
motif within the so-called NODD and CODD fragments of HIF-1α [23]. The same motif was …

… reveal a structural basis that … to pVHL with a motif similar to that of HIF-1α. A complex of
hydroxylated HIF-2α peptide (523–541) bound to VBC trimer was co-crystallized and the structure …

… L163R variants of pVHL inserted in VBC: HIF-1α complexes, … fragment from HIF-1α containing
either hydroxyproline Hyp564 … may be guiding HIF-1α recognition and proper positioning. …

… epitope of hydroxyproline is the key to the VHL recognition of … critical for interaction with
hydroxyproline 564 within CODD … and have contact with the hydroxyproline on CODD. We found …

… HIF-1α/-2α being the best characterized) and three PHDs. The PHD-catalysed hydroxylations
of HIF-1α/… We therefore worked to obtain structural information on how the different ODDs …

… P138R and L163R in pVHL appears not to 293 considerably disrupt HIF-1α binding to VBC
… 337 HIF-1α recognition and proper positioning. Introduction of both variants in pVHL induce …

… of full-length HIF-1α P402 and P564 hydroxyproline mutants that were the basis for the ODD
… VHL’s role as a substrate recognition subunit in an SCF-like protein degradation complex …

… Norma Masson and the lab of Professor Peter Ratcliffe for the provision of full-length HIF-
¡ ¢£¤¥ ¦§ P564 hydroxyproline mutants that were the basis for the ODD mutants used in this …

… To test whether prolyl-hydroxylation might alter the recognition of Akt1 by pVHL, we
performed in vitro binding assays with biotinylated Akt1-derived peptides. Peptides spanning the …