Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structure of Human Tyrosinase Related Protein 1 Reveals a Binuclear Zinc Active Site Important for Melanogenesis.

Angewandte Chemie (International ed. in English) - 7 Aug 2017

Lai Xuelei, Wichers Harry J, Soler-Lopez Montserrat, Dijkstra Bauke W

Abstract excerpt

Tyrosinase-related protein 1 (TYRP1) is one of three tyrosinase-like glycoenzymes in human melanocytes that are key to the production of melanin, the compound responsible for the pigmentation of skin, eye, and hair. Difficulties with producing these enzymes in pure form have hampered the understanding of their activity and the effect of mutations that cause albinism and pigmentation disorders. Herein we show that...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding Sites
Share to TYRP1 gene

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Membrane Glycoproteins

Share to Models, Molecular

Share to Mutation

Share to Oxidoreductases

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 28661582
DOI: 10.1002/anie.201704616
PMCID: PMC5601231

Genes

TYRP1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure of Human Tyrosinase Related Protein 1 Reveals a Binuclear Zinc Active Site Important for Melanogenesis.PMID 28661582Read ↗

Structure and Function of Human Tyrosinase and Tyrosinase-Related Proteins.Semantic proximity Read ↗

In vitro characterization of the intramelanosomal domain of human recombinant TYRP1 and its oculocutaneous albinism type 3-related mutant variants.Semantic proximity Read ↗

Computational analysis of histidine mutations on the structural stability of human tyrosinases leading to albinism insurgence.Semantic proximity Read ↗

Mutational analysis of copper binding by human tyrosinase.Semantic proximity Read ↗

Tyrp1 and oculocutaneous albinism type 3.Semantic proximity Read ↗

Identification of active site residues involved in metal cofactor binding and stereospecific substrate recognition in Mammalian tyrosinase. Implications to the catalytic cycle.Semantic proximity Read ↗

A three-dimensional model of mammalian tyrosinase active site accounting for loss of function mutations.Semantic proximity Read ↗

Tyrosinase gene (TYR) mutations in Chinese patients with oculocutaneous albinism type 1.Semantic proximity Read ↗

Type-3 copper proteins: recent advances on polyphenol oxidases.Semantic proximity Read ↗

Computational analysis of the deleterious non-synonymous single nucleotide polymorphisms (nsSNPs) in TYR gene impacting human tyrosinase protein and the protein stability.Semantic proximity Read ↗

Mutational analysis of TYR gene and its structural consequences in OCA1A.Semantic proximity Read ↗

Analysis of Immobilized Protein Unfolding and Molecular Dynamics Shows How pH, Glycosylation, and OCA3-Related Variants Influence Tyrp1's Stability and Function.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.