Structural enzymology binding studies of the peptide-substrate-binding domain of human collagen prolyl 4-hydroxylase (type-II): High affinity peptides have a PxGP sequence motif.

ABSTRACT: The peptide-substrate-binding (PSB) domain of collagen prolyl 4-hydroxylase (C-P4H, an α₂ β₂ tetramer) binds proline-rich procollagen peptides. This helical domain (the middle domain of the α subunit) has an important role concerning the substrate binding properties of C-P4H, although it is not known how the PSB domain influences the hydroxylation properties of the catalytic domain (the C-terminal domain of the α subunit). The crystal structures of the PSB domain of the human C-P4H isoform II (PSB-II) complexed with and without various short proline-rich peptides are described. The comparison with the previously determined PSB-I peptide complex structures shows that the C-P4H-I substrate peptide (PPG)₃ , has at most very weak affinity for PSB-II, although i

SUBMITTER: Murthy AV 

PROVIDER: S-EPMC6194285 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature