3i17
From Proteopedia
Crystal structure of the apo R132K:L121E mutant of cellular retinoic acid-binding protein II at 1.68 angstrom resolution
Structural highlights
FunctionRABP2_HUMAN Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCellular 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 structure of the R132K:L121E-CRABPII (PDB-3I17) double mutant suggests a direct interaction between engineered Glu121 and the native Arg111, which is critical for both Schiff base formation and protonation. Proteins 2009. (c) 2009 Wiley-Liss, Inc. Elucidating the exact role of engineered CRABPII residues for the formation of a retinal protonated Schiff base.,Vasileiou C, Wang W, Jia X, Lee KS, Watson CT, Geiger JH, Borhan B Proteins. 2009 Jun 8. PMID:19603486[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also
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