7YF1

Structure of FABP at 1.7 Angstroms resolution.

Summary for 7YF1

• Entry DOI: 10.2210/pdb7yf1/pdb
• Descriptor: Fatty acid-binding protein, heart, PALMITIC ACID (3 entities in total)
• Functional Keywords: fabp, lipid binding protein
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 1
• Total formula weight: 16067.26

Authors

Liu, Y.h.,Wang, L.l. (deposition date: 2022-07-07, release date: 2022-09-21, Last modification date: 2023-11-29)

Primary citation

Wang, L.,Zhang, H.,Lv, P.,Li, Y.,Teng, M.,Liu, Y.,Wu, D.
Structural Insights into Mouse H-FABP.
Life, 12:-, 2022

PubMed Abstract: 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 () 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.

PubMed: 36143481
DOI: 10.3390/life12091445

Experimental method

X-RAY DIFFRACTION (1.7 Å)