Title : Structural insights into the catalytic mechanism of cyclophilin A.

Pub. Date : 2003 Jun

PMID : 12730686






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 They possess both sequence-specific binding and proline cis-trans isomerase activities, as exemplified by the interaction between cyclophilin A (CypA) and the HIV-1 CA protein. Proline peptidylprolyl isomerase A Homo sapiens
2 They possess both sequence-specific binding and proline cis-trans isomerase activities, as exemplified by the interaction between cyclophilin A (CypA) and the HIV-1 CA protein. Proline peptidylprolyl isomerase A Homo sapiens
3 Here, we report crystal structures of CypA in complex with HIV-1 CA protein variants that bind preferentially with the substrate proline residue in either the cis or the trans conformation. Proline peptidylprolyl isomerase A Homo sapiens
4 CypA Arg55 guanidinium group probably facilitates catalysis by anchoring the substrate proline oxygen and stabilizing sp3 hybridization of the proline nitrogen in the transition state. Proline peptidylprolyl isomerase A Homo sapiens
5 CypA Arg55 guanidinium group probably facilitates catalysis by anchoring the substrate proline oxygen and stabilizing sp3 hybridization of the proline nitrogen in the transition state. Proline peptidylprolyl isomerase A Homo sapiens