1rmh: Difference between revisions

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[[Image:1rmh.gif|left|200px]]
{{Seed}}
[[Image:1rmh.png|left|200px]]


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{{STRUCTURE_1rmh|  PDB=1rmh  |  SCENE=  }}  
{{STRUCTURE_1rmh|  PDB=1rmh  |  SCENE=  }}  


'''RECOMBINANT CYCLOPHILIN A FROM HUMAN T CELL'''
===RECOMBINANT CYCLOPHILIN A FROM HUMAN T CELL===




==Overview==
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The crystal structure of human recombinant cyclophilin A complexed with a substrate of succinyl-Ala-Ala-Pro-Phe-p-nitroanilide (AAPF) has been determined and refined to an R-factor of 0.189 at 2.4 A resolution. The structure revealed only the cis form of the substrate bound to cyclophilin A in a stoichiometry of 1:1. This binding ratio is different from the structure of cyclophilin A complexed with the tetrapeptide N-acetyl-Ala-Ala-Pro-Ala-amidomethylcourmarin. Model docking revealed that the trans form of AAPF does not fit into the active site. The observation that only the trans cis form of AAPF binds to cyclophilin A implies that cyclophilin A predominantly catalyzes the trans to cis isomerization of a peptidylprolyl amide bond. On the basis of the structure, it is proposed that Arg55 hydrogen-bonds to the nitrogen to deconjugate the resonance of the prolyl amide bond and thus facilitates the cis-trans rotation.
The line below this paragraph, {{ABSTRACT_PUBMED_8652511}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_8652511}}


==About this Structure==
==About this Structure==
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[[Category: Ke, H.]]
[[Category: Ke, H.]]
[[Category: Zhao, Y.]]
[[Category: Zhao, Y.]]
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