title: Fatty acid induced remodeling within the human liver fatty acid-binding protein.
abstract: We crystallized human liver fatty acid-binding protein (LFABP) in apo, holo, and intermediate states of palmitic acid engagement. Structural snapshots of fatty acid recognition, entry, and docking within LFABP support a heads-in mechanism for ligand entry. Apo-LFABP undergoes structural remodeling, where the first palmitate ingress creates the atomic environment for placement of the second palmitate. These new mechanistic insights will facilitate development of pharmacological agents against LFABP.
authors.affiliation: Structural and Computational Biology Group, International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Road, 110067 New Delhi, India.
authors.forename: Ashwani
authors.initials: A
authors.lastname: Sharma
authors.forename: Amit
authors.initials: A
authors.lastname: Sharma
mesh_terms: D001059:Apoproteins; D003460:Crystallization; D018360:Crystallography, X-Ray; D050556:Fatty Acid-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D005227:Fatty Acids / Q000378:metabolism*; D006801:Humans; D008956:Models, Chemical; D010168:Palmitates / Q000737:chemistry*; D011485:Protein Binding
chemical_list: D001059:Apoproteins; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids; D010168:Palmitates