3stm | pdb_00003stm
From Proteopedia
Structure of human LFABP in complex with one molecule of palmitic acid
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Structural highlights
Function[FABPL_HUMAN] Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport. Publication Abstract from PubMedWe 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 first palmitate ingress creates atomic environment for placement of second palmitate. These new mechanistic insights will facilitate development of pharmacological agents against LFABP. Fatty acid induced remodeling within the Human liver fatty acid binding protein.,Sharma A, Sharma A J Biol Chem. 2011 Jul 8. PMID:21757748[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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