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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...

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Autores principales: Wang, Lili, Zhang, Haoran, Lv, Panjing, Li, Yan, Teng, Maikun, Liu, Yahui, Wu, Donghai
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
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.
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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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