Elucidating the exact role of engineered CRABPII residues for the formation of a retinal protonated Schiff base.
Elucidating the exact role of engineered CRABPII residues for the formation of a retinal protonated Schiff base.
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DOI:
10.1002/prot.22495
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发表时间:
2009-12
影响因子:
2.9
通讯作者:
Borhan, Babak
中科院分区:
文献类型:
--
作者:
Vasileiou, Chrysoula;Wang, Wenjing;Jia, Xiaofei;Lee, Kin Sing Stephen;Watson, Camille T.;Geiger, James H.;Borhan, Babak
关键词:
Cellular Retinoic Acid Binding Protein II (CRABPII) has been re-engineered 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, 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 double mutant suggests a direct interaction between engineered Glu121 and the native Arg111, which is critical for both Schiff base formation and protonation.
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影响因子:
3.3
作者:
BLATZ, PE;BAUMGARTNER, N;STEDMAN, E
通讯作者:
STEDMAN, E
影响因子:
15
作者:
GAT, Y;SHEVES, M
通讯作者:
SHEVES, M
DOI:
10.1107/s0907444904019158
发表时间:
2004-12-01
影响因子:
2.2
作者:
Emsley, P;Cowtan, K
通讯作者:
Cowtan, K
影响因子:
5.7
作者:
KLEYWEGT, GJ;BERGFORS, T;JONES, TA
通讯作者:
JONES, TA
影响因子:
3.4
作者:
BLATZ, PE;LIEBMAN, PA
通讯作者:
LIEBMAN, PA