1zmf

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(New page: 200px<br /> <applet load="1zmf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zmf, resolution 1.88&Aring;" /> '''C domain of human c...)
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'''C domain of human cyclophilin-33(hcyp33)'''<br />
'''C domain of human cyclophilin-33(hcyp33)'''<br />
==Overview==
==Overview==
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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.
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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==
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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].
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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]]
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[[Category: Chang, W.R.]]
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[[Category: Chang, W R.]]
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[[Category: Gu, S.Y.]]
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[[Category: Gu, S Y.]]
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[[Category: Liang, D.C.]]
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[[Category: Liang, D C.]]
[[Category: Wang, T.]]
[[Category: Wang, T.]]
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[[Category: Yun, C.H.]]
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[[Category: Yun, C H.]]
[[Category: human cyclophilin-33]]
[[Category: human cyclophilin-33]]
[[Category: ppiase]]
[[Category: ppiase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:36:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:16:59 2008''

Revision as of 14:17, 21 February 2008


1zmf, resolution 1.88Å

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C domain of human cyclophilin-33(hcyp33)

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.

About this Structure

1ZMF is a Single protein structure of sequence from Homo sapiens. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 Full crystallographic information is available from OCA.

Reference

1.88 A crystal structure of the C domain of hCyP33: a novel domain of peptidyl-prolyl cis-trans isomerase., Wang T, Yun CH, Gu SY, Chang WR, Liang DC, Biochem Biophys Res Commun. 2005 Aug 5;333(3):845-9. PMID:15963461

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