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Further advances in the production of membrane proteins in Pichia pastoris

Membrane proteins have essential cellular functions and are therefore of high interest in both academia and industry. Many efforts have been made on producing those targets in yields allowing crystallization experiments aiming for high resolution structures and mechanistic understanding. The first s...

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Detalles Bibliográficos
Autor principal: Hedfalk, Kristina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3937196/
https://www.ncbi.nlm.nih.gov/pubmed/23507631
http://dx.doi.org/10.4161/bioe.23886
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author Hedfalk, Kristina
author_facet Hedfalk, Kristina
author_sort Hedfalk, Kristina
collection PubMed
description Membrane proteins have essential cellular functions and are therefore of high interest in both academia and industry. Many efforts have been made on producing those targets in yields allowing crystallization experiments aiming for high resolution structures and mechanistic understanding. The first step of production provides a crucial barrier to overcome, but what we now see, is great progress in membrane protein structural determination in a relatively short time. Achievements on recombinant protein production have been essential for this development and the yeast Pichia pastoris is the most commonly used host for eukaryotic membrane proteins. High-resolution structures nicely illustrate the successes in protein production, and this is the measure used by Ramón and Marin in their review “Advances in the production of membrane proteins in Pichia pastoris” from 2011. Here, additional advances on production and crystallization of eukaryotic membrane proteins are described and reflected on.
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spelling pubmed-39371962014-03-06 Further advances in the production of membrane proteins in Pichia pastoris Hedfalk, Kristina Bioengineered Commentary Membrane proteins have essential cellular functions and are therefore of high interest in both academia and industry. Many efforts have been made on producing those targets in yields allowing crystallization experiments aiming for high resolution structures and mechanistic understanding. The first step of production provides a crucial barrier to overcome, but what we now see, is great progress in membrane protein structural determination in a relatively short time. Achievements on recombinant protein production have been essential for this development and the yeast Pichia pastoris is the most commonly used host for eukaryotic membrane proteins. High-resolution structures nicely illustrate the successes in protein production, and this is the measure used by Ramón and Marin in their review “Advances in the production of membrane proteins in Pichia pastoris” from 2011. Here, additional advances on production and crystallization of eukaryotic membrane proteins are described and reflected on. Landes Bioscience 2013-11-01 2013-03-18 /pmc/articles/PMC3937196/ /pubmed/23507631 http://dx.doi.org/10.4161/bioe.23886 Text en Copyright © 2013 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Commentary
Hedfalk, Kristina
Further advances in the production of membrane proteins in Pichia pastoris
title Further advances in the production of membrane proteins in Pichia pastoris
title_full Further advances in the production of membrane proteins in Pichia pastoris
title_fullStr Further advances in the production of membrane proteins in Pichia pastoris
title_full_unstemmed Further advances in the production of membrane proteins in Pichia pastoris
title_short Further advances in the production of membrane proteins in Pichia pastoris
title_sort further advances in the production of membrane proteins in pichia pastoris
topic Commentary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3937196/
https://www.ncbi.nlm.nih.gov/pubmed/23507631
http://dx.doi.org/10.4161/bioe.23886
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