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Structural Insights into Mouse H-FABP
Intracellular fatty acid-binding proteins are evolutionarily highly conserved proteins. The major functions and responsibilities of this family are the regulation of FA uptake and intracellular transport. The structure of the H-FABP ortholog from mouse (Mus musculus) had not been revealed at the tim...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9505153/ https://www.ncbi.nlm.nih.gov/pubmed/36143481 http://dx.doi.org/10.3390/life12091445 |
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author | Wang, Lili Zhang, Haoran Lv, Panjing Li, Yan Teng, Maikun Liu, Yahui Wu, Donghai |
author_facet | Wang, Lili Zhang, Haoran Lv, Panjing Li, Yan Teng, Maikun Liu, Yahui Wu, Donghai |
author_sort | Wang, Lili |
collection | PubMed |
description | Intracellular fatty acid-binding proteins are evolutionarily highly conserved proteins. The major functions and responsibilities of this family are the regulation of FA uptake and intracellular transport. The structure of the H-FABP ortholog from mouse (Mus musculus) had not been revealed at the time this study was completed. Thus, further exploration of the structural properties of mouse H-FABP is expected to extend our knowledge of the model animal’s molecular mechanism of H-FABP function. Here, we report the high-resolution crystal structure and the NMR characterization of mouse H-FABP. Our work discloses the unique structural features of mouse H-FABP, offering a structural basis for the further development of small-molecule inhibitors for H-FABP. |
format | Online Article Text |
id | pubmed-9505153 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-95051532022-09-24 Structural Insights into Mouse H-FABP Wang, Lili Zhang, Haoran Lv, Panjing Li, Yan Teng, Maikun Liu, Yahui Wu, Donghai Life (Basel) Article Intracellular fatty acid-binding proteins are evolutionarily highly conserved proteins. The major functions and responsibilities of this family are the regulation of FA uptake and intracellular transport. The structure of the H-FABP ortholog from mouse (Mus musculus) had not been revealed at the time this study was completed. Thus, further exploration of the structural properties of mouse H-FABP is expected to extend our knowledge of the model animal’s molecular mechanism of H-FABP function. Here, we report the high-resolution crystal structure and the NMR characterization of mouse H-FABP. Our work discloses the unique structural features of mouse H-FABP, offering a structural basis for the further development of small-molecule inhibitors for H-FABP. MDPI 2022-09-16 /pmc/articles/PMC9505153/ /pubmed/36143481 http://dx.doi.org/10.3390/life12091445 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Wang, Lili Zhang, Haoran Lv, Panjing Li, Yan Teng, Maikun Liu, Yahui Wu, Donghai Structural Insights into Mouse H-FABP |
title | Structural Insights into Mouse H-FABP |
title_full | Structural Insights into Mouse H-FABP |
title_fullStr | Structural Insights into Mouse H-FABP |
title_full_unstemmed | Structural Insights into Mouse H-FABP |
title_short | Structural Insights into Mouse H-FABP |
title_sort | structural insights into mouse h-fabp |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9505153/ https://www.ncbi.nlm.nih.gov/pubmed/36143481 http://dx.doi.org/10.3390/life12091445 |
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