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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Bibliographic Details
Published in:Life (Basel, Switzerland) Switzerland), 2022-09, Vol.12 (9), p.1445
Main Authors: Wang, Lili, Zhang, Haoran, Lv, Panjing, Li, Yan, Teng, Maikun, Liu, Yahui, Wu, Donghai
Format: Article
Language:English
Subjects:
Biomarkers
Cardiomyocytes
Chromatography
Crystal structure
Crystals
E coli
Enzymes
Experiments
Fatty acid-binding protein
Fatty acids
Glycerol
Heart failure
Intracellular
mouse H-FABP
Musculoskeletal system
NMR
NMR structure
Nuclear magnetic resonance
Plasmids
Protein expression
Proteins
Structural analysis
structural biology
X-rays
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Summary: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.
ISSN:2075-1729
2075-1729
DOI:10.3390/life12091445