ArticleThe EMBO journal1999
Identification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylase.
Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 79 citations in OpenAlex.
- P4HA3 is dispensable for prolyl 4-hydroxylation of type I collagen during mouse development.The Journal of biological chemistry · 2026Article
- Targeting collagen biosynthesis by small molecules inhibiting the function of the peptide-substrate-binding domain of collagen prolyl 4-hydroxylases.Scientific reports · 2026Article
- Evidence for the major role of PH4⍺EFB in the prolyl 4-hydroxylation of Drosophila collagen IV.Matrix biology : journal of the International Society for Matrix Biology · 2025Article
- Article
- Enhanced Collagen Prolyl 4-Hydroxylase Activity and Expression Promote Cancer Progression via Both Canonical and Non-Canonical Mechanisms.International journal of molecular sciences · 2025Review
- Collagen IV biosynthesis: Intracellular choreography of post-translational modifications.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- Comprehensive analysis of the effects ofFrontiers in cell and developmental biology · 2025Article
- Reduced Bone Mass in Collagen Prolyl 4-HydroxylaseJBMR plus · 2022Article
- Role of prolyl hydroxylation in the molecular interactions of collagens.Essays in biochemistry · 2019Review
- 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.Protein science : a publication of the Protein Society · 2018Article
- Pathway Analysis of Gene Expression in Murine Fetal and Adult Wounds.Advances in wound care · 2018Article
- Bacillus anthracis Prolyl 4-Hydroxylase Modifies Collagen-like Substrates in Asymmetric Patterns.The Journal of biological chemistry · 2016Article
- Hypoxia-inducible factor-1 (HIF-1) but not HIF-2 is essential for hypoxic induction of collagen prolyl 4-hydroxylases in primary newborn mouse epiphyseal growth plate chondrocytes.The Journal of biological chemistry · 2012Article
- Deficiency of a transmembrane prolyl 4-hydroxylase in the zebrafish leads to basement membrane defects and compromised kidney function.The Journal of biological chemistry · 2010Article
- Crystal structure of prolyl 4-hydroxylase from Bacillus anthracis.Biochemistry · 2010Article
- Prolyl 4-hydroxylation of alpha-fibrinogen: a novel protein modification revealed by plasma proteomics.The Journal of biological chemistry · 2009Article
- Identification and characterization of a novel human hepatocellular carcinoma-associated gene.British journal of cancer · 2001Article
- Post-translational hydroxylation at the N-terminus of the prion protein reveals presence of PPII structure in vivo.The EMBO journal · 2000Article
- Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
unlabelledProlyl 4-hydroxylase (EC 1.14.11.2) catalyzes the hydroxylation of -X-Pro-Gly- sequences and plays a central role in the synthesis of all collagens. The [alpha(I)]2beta2 type I enzyme is effectively inhibited by poly(L-proline), whereas the [alpha(II)]2beta2 type II enzyme is not. We report here that the poly(L-proline) and (Pro-Pro-Gly)10 peptide substrate-binding domain of prolyl 4-hydroxylase is distinct from the catalytic domain and consists of approximately 100 amino acids. Peptides of 10-19 kDa beginning around residue 140 in the 517 residue alpha(I) subunit remained bound to poly(L-proline) agarose after limited proteolysis of the human type I enzyme tetramer. A recombinant polypeptide corresponding to the alpha(I) subunit residues 138-244 and expressed in Escherichia coli was soluble, became effectively bound to poly(L-proline) agarose and could be eluted with (Pro-Pro-Gly)10. This polypeptide is distinct from the SH3 and WW domains, and from profilin, and thus represents a new type of proline-rich peptide-binding module. Studies with enzyme tetramers containing mutated alpha subunits demonstrated that the presence of a glutamate and a glutamine in the alpha(II) subunit in the positions corresponding to Ile182 and Tyr233 in the alpha(I) subunit explains most of the lack of poly(L-proline) binding of the type II prolyl 4-hydroxylase. KEYWORDS: collagen/dioxygenases/peptide-binding domain/ proline-rich/prolyl hydroxylase
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