6L7K
solution structure of hIFABP V60C/Y70C variant.
Summary for 6L7K
| Entry DOI | 10.2210/pdb6l7k/pdb |
| Descriptor | Fatty acid-binding protein, intestinal (1 entity in total) |
| Functional Keywords | fatty acid binding protein, mutant, disulfide, transport protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 15042.02 |
| Authors | |
| Primary citation | Xiao, T.,Lu, Y.,Fan, J.S.,Yang, D. Ligand Entry into Fatty Acid Binding Protein via Local Unfolding Instead of Gap Widening. Biophys.J., 118:396-402, 2020 Cited by PubMed Abstract: Fatty acid binding proteins play an important role in the transportation of fatty acids. Despite intensive studies, how fatty acids enter the protein cavity for binding is still controversial. Here, a gap-closed variant of human intestinal fatty acid binding protein was generated by mutagenesis, in which the gap is locked by a disulfide bridge. According to its structure determined here by NMR, this variant has no obvious openings as the ligand entrance and the gap cannot be widened by internal dynamics. Nevertheless, it still takes up fatty acids and other ligands. NMR relaxation dispersion, chemical exchange saturation transfer, and hydrogen-deuterium exchange experiments show that the variant exists in a major native state, two minor native-like states, and two locally unfolded states in aqueous solution. Local unfolding of either βB-βD or helix 2 can generate an opening large enough for ligands to enter the protein cavity, but only the fast local unfolding of helix 2 is relevant to the ligand entry process. PubMed: 31870540DOI: 10.1016/j.bpj.2019.12.005 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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