Journal
LIFE-BASEL
Volume 12, Issue 9, Pages -Publisher
MDPI
DOI: 10.3390/life12091445
Keywords
mouse H-FABP; crystal structure; NMR structure; structural biology
Categories
Funding
- Guangzhou International Collaborative [2019A050510027]
- National Science Foundation of China [30811120429]
- National Basic Research Program of China [2010CB9455000]
- China Postdoctoral Science Foundation [2020M682420]
- China-New Zealand Joint Laboratory on Biomedicine and Health
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Intracellular fatty acid-binding proteins are highly conserved proteins with important functions in regulating fatty acid uptake and intracellular transport. This study reveals the unique structural features of mouse H-FABP, providing a basis for the development of small-molecule inhibitors for 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 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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