作者: Leonard Banaszak , Nathan Winter , Zhaohui Xu , David A. Bernlohr , Sandra Cowan
DOI: 10.1016/S0065-3233(08)60639-7
关键词: Structural motif 、 Peptide sequence 、 Lysophospholipids 、 Fatty acid 、 Biochemistry 、 Transport protein 、 Protein family 、 Extracellular 、 Biology 、 Fatty acid-binding protein
摘要: Publisher Summary This chapter focuses on the structural analyses and comparisons between members of a multigene family hydrophobic ligand-binding proteins. It discusses motif, general characteristics binding cavity, ligand entry, portal hypothesis provides detailed comparison intra- extracellular lipid proteins with known crystal structures. The this are referred as lipid-binding (LBPs). collection can be subdivided into two groups: intracellular protein (iLBP) (eLBP). primarily deals iLBP branch because is becoming structurally well characterized. However, extended to some eLBP basic motif used bind ligands applies both. products hydrolysis intestinal lipids, including fatty acids, cholesterol, monoglycerides, lysophospholipids, have very low solubilities absorbed by biliary micelles in gut. These diffuse through glycocalyx, which stabilizes an unstirred water layer at surface enterocyte. concludes discussion results site-directed mutagenesis studies, thermodynamics binding, considerations stability folding.