Cargando…

Cisplatin Binding to Human Serum Transferrin: A Crystallographic Study

[Image: see text] The molecular mechanism of how human serum transferrin (hTF) recognizes cisplatin at the atomic level is still unclear. Here, we report the molecular structure of the adduct formed upon the reaction of hTF with cisplatin. Pt binds the side chain of Met256 (at the N-lobe), without a...

Descripción completa

Detalles Bibliográficos
Autores principales: Troisi, Romualdo, Galardo, Francesco, Ferraro, Giarita, Sica, Filomena, Merlino, Antonello
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2023
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9846693/
https://www.ncbi.nlm.nih.gov/pubmed/36602395
http://dx.doi.org/10.1021/acs.inorgchem.2c04206
_version_ 1784871247706849280
author Troisi, Romualdo
Galardo, Francesco
Ferraro, Giarita
Sica, Filomena
Merlino, Antonello
author_facet Troisi, Romualdo
Galardo, Francesco
Ferraro, Giarita
Sica, Filomena
Merlino, Antonello
author_sort Troisi, Romualdo
collection PubMed
description [Image: see text] The molecular mechanism of how human serum transferrin (hTF) recognizes cisplatin at the atomic level is still unclear. Here, we report the molecular structure of the adduct formed upon the reaction of hTF with cisplatin. Pt binds the side chain of Met256 (at the N-lobe), without altering the protein overall conformation.
format Online
Article
Text
id pubmed-9846693
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher American Chemical Society
record_format MEDLINE/PubMed
spelling pubmed-98466932023-01-19 Cisplatin Binding to Human Serum Transferrin: A Crystallographic Study Troisi, Romualdo Galardo, Francesco Ferraro, Giarita Sica, Filomena Merlino, Antonello Inorg Chem [Image: see text] The molecular mechanism of how human serum transferrin (hTF) recognizes cisplatin at the atomic level is still unclear. Here, we report the molecular structure of the adduct formed upon the reaction of hTF with cisplatin. Pt binds the side chain of Met256 (at the N-lobe), without altering the protein overall conformation. American Chemical Society 2023-01-05 /pmc/articles/PMC9846693/ /pubmed/36602395 http://dx.doi.org/10.1021/acs.inorgchem.2c04206 Text en © 2023 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Troisi, Romualdo
Galardo, Francesco
Ferraro, Giarita
Sica, Filomena
Merlino, Antonello
Cisplatin Binding to Human Serum Transferrin: A Crystallographic Study
title Cisplatin Binding to Human Serum Transferrin: A Crystallographic Study
title_full Cisplatin Binding to Human Serum Transferrin: A Crystallographic Study
title_fullStr Cisplatin Binding to Human Serum Transferrin: A Crystallographic Study
title_full_unstemmed Cisplatin Binding to Human Serum Transferrin: A Crystallographic Study
title_short Cisplatin Binding to Human Serum Transferrin: A Crystallographic Study
title_sort cisplatin binding to human serum transferrin: a crystallographic study
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9846693/
https://www.ncbi.nlm.nih.gov/pubmed/36602395
http://dx.doi.org/10.1021/acs.inorgchem.2c04206
work_keys_str_mv AT troisiromualdo cisplatinbindingtohumanserumtransferrinacrystallographicstudy
AT galardofrancesco cisplatinbindingtohumanserumtransferrinacrystallographicstudy
AT ferrarogiarita cisplatinbindingtohumanserumtransferrinacrystallographicstudy
AT sicafilomena cisplatinbindingtohumanserumtransferrinacrystallographicstudy
AT merlinoantonello cisplatinbindingtohumanserumtransferrinacrystallographicstudy