1rmh

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[[Image:1rmh.gif|left|200px]]<br /><applet load="1rmh" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rmh.gif|left|200px]]
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caption="1rmh, resolution 2.4&Aring;" />
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'''RECOMBINANT CYCLOPHILIN A FROM HUMAN T CELL'''<br />
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{{Structure
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|PDB= 1rmh |SIZE=350|CAPTION= <scene name='initialview01'>1rmh</scene>, resolution 2.4&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE= CYCLOPHILIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''RECOMBINANT CYCLOPHILIN A FROM HUMAN T CELL'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1RMH is a [[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==
==Reference==
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Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization., Zhao Y, Ke H, Biochemistry. 1996 Jun 11;35(23):7356-61. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8652511 8652511]
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Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization., Zhao Y, Ke H, Biochemistry. 1996 Jun 11;35(23):7356-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8652511 8652511]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: complex (isomerase/substrate)]]
[[Category: complex (isomerase/substrate)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:53:34 2008''

Revision as of 11:53, 20 March 2008

Image:1rmh.gif


PDB ID 1rmh

Drag the structure with the mouse to rotate
, resolution 2.4Å
Gene: CYCLOPHILIN (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



RECOMBINANT CYCLOPHILIN A FROM HUMAN T CELL


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.

About this Structure

1RMH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization., Zhao Y, Ke H, Biochemistry. 1996 Jun 11;35(23):7356-61. PMID:8652511

Page seeded by OCA on Thu Mar 20 13:53:34 2008

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