Backbone and nearly complete side-chain chemical shift assignments reveal the human uncharacterized protein CXorf51A as intrinsically disordered

Even though the human genome project showed that our DNA contains a mere 20,000 to 25,000 protein coding genes, an unexpectedly large number of these proteins remain functionally uncharacterized. A structural characterization of these “unknown” proteins may help to identify possible cellular tasks....

Descripción completa

Detalles Bibliográficos
Autores principales: Wiedemann, Christoph, Obika, Kingsley Benjamin, Liebscher, Sandra, Jirschitzka, Jan, Ohlenschlãger, Oliver, Bordusa, Frank
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2021
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8481210/
https://www.ncbi.nlm.nih.gov/pubmed/34415548
http://dx.doi.org/10.1007/s12104-021-10043-6
_version_ 1784576635120386048
author Wiedemann, Christoph
Obika, Kingsley Benjamin
Liebscher, Sandra
Jirschitzka, Jan
Ohlenschlãger, Oliver
Bordusa, Frank
author_facet Wiedemann, Christoph
Obika, Kingsley Benjamin
Liebscher, Sandra
Jirschitzka, Jan
Ohlenschlãger, Oliver
Bordusa, Frank
author_sort Wiedemann, Christoph
collection PubMed
description Even though the human genome project showed that our DNA contains a mere 20,000 to 25,000 protein coding genes, an unexpectedly large number of these proteins remain functionally uncharacterized. A structural characterization of these “unknown” proteins may help to identify possible cellular tasks. We therefore used a combination of bioinformatics and nuclear magnetic resonance spectroscopy to structurally de-orphanize one of these gene products, the 108 amino acid human uncharacterized protein CXorf51A. Both our bioinformatics analysis as well as the [Formula: see text] H, [Formula: see text] C, [Formula: see text] N backbone and near-complete side-chain chemical shift assignments indicate that it is an intrinsically disordered protein.
format Online
Article
Text
id pubmed-8481210
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher Springer Netherlands
record_format MEDLINE/PubMed
spelling pubmed-84812102021-10-08 Backbone and nearly complete side-chain chemical shift assignments reveal the human uncharacterized protein CXorf51A as intrinsically disordered Wiedemann, Christoph Obika, Kingsley Benjamin Liebscher, Sandra Jirschitzka, Jan Ohlenschlãger, Oliver Bordusa, Frank Biomol NMR Assign Article Even though the human genome project showed that our DNA contains a mere 20,000 to 25,000 protein coding genes, an unexpectedly large number of these proteins remain functionally uncharacterized. A structural characterization of these “unknown” proteins may help to identify possible cellular tasks. We therefore used a combination of bioinformatics and nuclear magnetic resonance spectroscopy to structurally de-orphanize one of these gene products, the 108 amino acid human uncharacterized protein CXorf51A. Both our bioinformatics analysis as well as the [Formula: see text] H, [Formula: see text] C, [Formula: see text] N backbone and near-complete side-chain chemical shift assignments indicate that it is an intrinsically disordered protein. Springer Netherlands 2021-08-20 2021 /pmc/articles/PMC8481210/ /pubmed/34415548 http://dx.doi.org/10.1007/s12104-021-10043-6 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Wiedemann, Christoph
Obika, Kingsley Benjamin
Liebscher, Sandra
Jirschitzka, Jan
Ohlenschlãger, Oliver
Bordusa, Frank
Backbone and nearly complete side-chain chemical shift assignments reveal the human uncharacterized protein CXorf51A as intrinsically disordered
title Backbone and nearly complete side-chain chemical shift assignments reveal the human uncharacterized protein CXorf51A as intrinsically disordered
title_full Backbone and nearly complete side-chain chemical shift assignments reveal the human uncharacterized protein CXorf51A as intrinsically disordered
title_fullStr Backbone and nearly complete side-chain chemical shift assignments reveal the human uncharacterized protein CXorf51A as intrinsically disordered
title_full_unstemmed Backbone and nearly complete side-chain chemical shift assignments reveal the human uncharacterized protein CXorf51A as intrinsically disordered
title_short Backbone and nearly complete side-chain chemical shift assignments reveal the human uncharacterized protein CXorf51A as intrinsically disordered
title_sort backbone and nearly complete side-chain chemical shift assignments reveal the human uncharacterized protein cxorf51a as intrinsically disordered
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8481210/
https://www.ncbi.nlm.nih.gov/pubmed/34415548
http://dx.doi.org/10.1007/s12104-021-10043-6
work_keys_str_mv AT wiedemannchristoph backboneandnearlycompletesidechainchemicalshiftassignmentsrevealthehumanuncharacterizedproteincxorf51aasintrinsicallydisordered
AT obikakingsleybenjamin backboneandnearlycompletesidechainchemicalshiftassignmentsrevealthehumanuncharacterizedproteincxorf51aasintrinsicallydisordered
AT liebschersandra backboneandnearlycompletesidechainchemicalshiftassignmentsrevealthehumanuncharacterizedproteincxorf51aasintrinsicallydisordered
AT jirschitzkajan backboneandnearlycompletesidechainchemicalshiftassignmentsrevealthehumanuncharacterizedproteincxorf51aasintrinsicallydisordered
AT ohlenschlageroliver backboneandnearlycompletesidechainchemicalshiftassignmentsrevealthehumanuncharacterizedproteincxorf51aasintrinsicallydisordered
AT bordusafrank backboneandnearlycompletesidechainchemicalshiftassignmentsrevealthehumanuncharacterizedproteincxorf51aasintrinsicallydisordered

Ejemplares similares