Ontology highlight
ABSTRACT:
SUBMITTER: Vasileiou C
PROVIDER: S-EPMC4306427 | biostudies-literature | 2009 Dec
REPOSITORIES: biostudies-literature
Proteins 20091201 4
Cellular Retinoic Acid Binding Protein II (CRABPII) has been reengineered to specifically bind and react with all-trans-retinal to form a protonated Schiff base. Each step of this process has been dissected and four residues (Lys132, Tyr134, Arg111, and Glu121) within the CRABPII binding site have been identified as crucial for imine formation and/or protonation. The precise role of each residue has been examined through site directed mutagenesis and crystallographic studies. The crystal structu ...[more]