1zmf: Difference between revisions

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New page: left|200px<br /> <applet load="1zmf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zmf, resolution 1.88Å" /> '''C domain of human c...
 
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[[Image:1zmf.gif|left|200px]]<br />
[[Image:1zmf.gif|left|200px]]<br /><applet load="1zmf" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1zmf" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1zmf, resolution 1.88&Aring;" />
caption="1zmf, resolution 1.88&Aring;" />
'''C domain of human cyclophilin-33(hcyp33)'''<br />
'''C domain of human cyclophilin-33(hcyp33)'''<br />


==Overview==
==Overview==
Cyclophilins (CyPs) are a widespreading protein family in living organisms, and possess the activity of peptidyl-prolyl cis-trans isomerase (PPIase), which is inhibited by cyclosporin A (CsA). The human nuclear cyclophilin, (hCyP33) is the first protein which was found to contain two RNA binding, domains at the amino-terminus and a PPIase domain at the, carboxyl-terminus. We isolated the hCyP33 gene from the human, hematopoietic stem/progenitor cells and expressed it in Escherichia coli, and determined the crystal structure of the C domain of hCyP33 at 1.88 A, resolution. The core structure is a beta-barrel covered by two, alpha-helices. Superposition of the structure of the C domain of hCyP33, with the structure of CypA suggests that the C domain contains PPIase, active site which binds to CsA. Furthermore, C domain seems to be able to, bind with the Gag-encoded capsid (CA) of HIV-1 and may affect the viral, replication of HIV-1. A key residue of the active site is changed from, Ala-103-CypA to Ser-239-hCyP33, which may affect the PPIase, domain/substrates interactions.
Cyclophilins (CyPs) are a widespreading protein family in living organisms and possess the activity of peptidyl-prolyl cis-trans isomerase (PPIase), which is inhibited by cyclosporin A (CsA). The human nuclear cyclophilin (hCyP33) is the first protein which was found to contain two RNA binding domains at the amino-terminus and a PPIase domain at the carboxyl-terminus. We isolated the hCyP33 gene from the human hematopoietic stem/progenitor cells and expressed it in Escherichia coli, and determined the crystal structure of the C domain of hCyP33 at 1.88 A resolution. The core structure is a beta-barrel covered by two alpha-helices. Superposition of the structure of the C domain of hCyP33 with the structure of CypA suggests that the C domain contains PPIase active site which binds to CsA. Furthermore, C domain seems to be able to bind with the Gag-encoded capsid (CA) of HIV-1 and may affect the viral replication of HIV-1. A key residue of the active site is changed from Ala-103-CypA to Ser-239-hCyP33, which may affect the PPIase domain/substrates interactions.


==About this Structure==
==About this Structure==
1ZMF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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=1ZMF OCA].  
1ZMF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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=1ZMF OCA].  


==Reference==
==Reference==
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[[Category: Peptidylprolyl isomerase]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Chang, W.R.]]
[[Category: Chang, W R.]]
[[Category: Gu, S.Y.]]
[[Category: Gu, S Y.]]
[[Category: Liang, D.C.]]
[[Category: Liang, D C.]]
[[Category: Wang, T.]]
[[Category: Wang, T.]]
[[Category: Yun, C.H.]]
[[Category: Yun, C H.]]
[[Category: human cyclophilin-33]]
[[Category: human cyclophilin-33]]
[[Category: ppiase]]
[[Category: ppiase]]


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