Essentials of biorecognition: the (strept)avidin-biotin system as a model for protein-protein and protein-ligand interaction.
Molecular recognition or biorecognition is as the heart of all biological interactions. These interactions are characterized by a collection of noncovalent bonds, namely ionic, hydrogen-bonding and hydrophobic interactions. In addition, shape complementarity appears to play a pivotal role in the process of biorecognition. In this review, we examine the versatile avidin-biotin complex as a model system for study of the biorecognition phenomenon with respect to protein-protein, protein-peptide, protein-ligand and protein-DNA interactions.
Wilchek
Meir
M
Department of Biological Chemistry, The Weizmann Institute of Science, 76100 Rehovot, Israel. meir.wilchek@weizmann.ac.il
Bayer
Edward A
EA
Livnah
Oded
O
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001710:Biotin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism*; D008024:Ligands; D008954:Models, Biological; D008958:Models, Molecular; D011485:Protein Binding / Q000502:physiology; D019809:Streptavidin / Q000737:chemistry / Q000378:metabolism*
D001426:Bacterial Proteins; D008024:Ligands; C066114:biotin-streptavidin complex; D001710:Biotin; D019809:Streptavidin