ArticleInternational journal of molecular sciences2020
Phenylthiourea Binding to Human Tyrosinase-Related Protein 1.
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Analysis of Immobilized Protein Unfolding and Molecular Dynamics Shows How pH, Glycosylation, and OCA3-Related Variants Influence Tyrp1's Stability and Function.International journal of molecular sciences · 2026Article
- Discovery of Tyrosinase Inhibitors fromCurrent issues in molecular biology · 2026Article
- In-silico evaluation of potential plant-based tyrosinase inhibitors for cosmetic and pharmaceutical applications.Biotechnology letters · 2025Article
- Novel Hydrogenated Derivatives of Chemically Modified Curcumin CMC2.24 Are Potent Inhibitors of Melanogenesis in an In Vitro Model: Influence of Degree of Hydrogenation.Life (Basel, Switzerland) · 2023Article
- Recent Advances and Progress on Melanin: From Source to Application.International journal of molecular sciences · 2023Review
- Inhibitory Effect of Avenanthramides (Avn) on Tyrosinase Activity and Melanogenesis in α-MSH-Activated SK-MEL-2 Cells: In Vitro and In Silico Analysis.International journal of molecular sciences · 2021Article
- Synthesis and Studies of the Inhibitory Effect of Hydroxylated Phenylpropanoids and Biphenols Derivatives on Tyrosinase and Laccase Enzymes.Molecules (Basel, Switzerland) · 2020Article
- Photoprotection and Skin Pigmentation: Melanin-Related Molecules and Some Other New Agents Obtained from Natural Sources.Molecules (Basel, Switzerland) · 2020Review
- Medicinal Effect,Scientifica · 2020Review
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tyrosinase-related protein 1 (TYRP1) is one of the three human melanogenic enzymes involved in the biosynthesis of melanin, a pigment responsible for the color of the skin, hair, and eyes. It shares high sequence identity with tyrosinase, but has two zinc ions in its active site rather than two copper ions as in tyrosinase. Typical tyrosinase inhibitors do not directly coordinate to the zinc ions of TYRP1. Here, we show, from an X-ray crystal structure determination, that phenylthiourea, a highly potent tyrosinase inhibitor, does neither coordinate the active site zinc ions, but binds differently from other structurally characterized TYRP1-inhibitor complexes. Its aromatic ring is directed outwards from the active site, apparently as a result from the absence of polar oxygen substituents that can take the position of water molecules bound in the active site. The compound binds via hydrophobic interactions, thereby blocking substrate access to the active site.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.