1m9c: Difference between revisions

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[[Image:1m9c.gif|left|200px]]<br />
[[Image:1m9c.gif|left|200px]]<br /><applet load="1m9c" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1m9c" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1m9c, resolution 2.00&Aring;" />
caption="1m9c, resolution 2.00&Aring;" />
'''X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type Complex.'''<br />
'''X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type Complex.'''<br />


==Overview==
==Overview==
Cyclophilins constitute a ubiquitous protein family whose functions, include protein folding, transport and signaling. 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. 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. Cis- and, trans-Pro substrates are accommodated within the enzyme active site by, rearrangement of their N-terminal residues and with minimal distortions in, the path of the main chain. 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.
Cyclophilins constitute a ubiquitous protein family whose functions include protein folding, transport and signaling. 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. 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. Cis- and trans-Pro substrates are accommodated within the enzyme active site by rearrangement of their N-terminal residues and with minimal distortions in the path of the main chain. 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.


==About this Structure==
==About this Structure==
1M9C is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M9C OCA].  
1M9C is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M9C OCA].  


==Reference==
==Reference==
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[[Category: Peptidylprolyl isomerase]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Hill, C.P.]]
[[Category: Hill, C P.]]
[[Category: Howard, B.R.]]
[[Category: Howard, B R.]]
[[Category: Li, S.]]
[[Category: Li, S.]]
[[Category: Sundquist, W.I.]]
[[Category: Sundquist, W I.]]
[[Category: Vajdos, F.F.]]
[[Category: Vajdos, F F.]]
[[Category: capsid]]
[[Category: capsid]]
[[Category: cyclophilin a]]
[[Category: cyclophilin a]]
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[[Category: rotamase]]
[[Category: rotamase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:09:00 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:52:51 2008''