1rmh: Difference between revisions

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[[Image:1rmh.gif|left|200px]]<br /><applet load="1rmh" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1rmh.gif|left|200px]]<br /><applet load="1rmh" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1rmh, resolution 2.4Å" />

'''RECOMBINANT CYCLOPHILIN A FROM HUMAN T CELL'''<br />

==Overview==

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 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.

==About this Structure==

1RMH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1RMH OCA].

1RMH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RMH OCA].

==Reference==

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[[Category: complex (isomerase/substrate)]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 01:42:~~40 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:26 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1rmh.gif|left|200px]]<br /><applet load="1rmh" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1rmh.gif|left|200px]]<br /><applet load="1rmh" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1rmh, resolution 2.4&Aring;" />
 '''RECOMBINANT CYCLOPHILIN A FROM HUMAN T CELL'''<br />
 ==Overview==
-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 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.
 ==About this Structure==
-RMH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RMH OCA].
+RMH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RMH OCA].
 ==Reference==
@@ Line 17: / Line 17: @@
 [[Category: complex (isomerase/substrate)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:42:40 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:26 2008''