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| {{STRUCTURE_2ose| PDB=2ose | SCENE= }} | | {{STRUCTURE_2ose| PDB=2ose | SCENE= }} |
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| '''Crystal Structure of the Mimivirus Cyclophilin'''
| | ===Crystal Structure of the Mimivirus Cyclophilin=== |
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| ==Overview==
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| Although multiple viruses utilize host cell cyclophilins, including severe acute respiratory syndrome (SARS) and human immunodeficiency virus type-1(HIV-1), their role in infection is poorly understood. To help elucidate these roles, we have characterized the first virally encoded cyclophilin (mimicyp) derived from the largest virus discovered to date (the Mimivirus) that is also a causative agent of pneumonia in humans. Mimicyp adopts a typical cyclophilin-fold, yet it also forms trimers unlike any previously characterized homologue. Strikingly, immunofluorescence assays reveal that mimicyp localizes to the surface of the mature virion, as recently proposed for several viruses that recruit host cell cyclophilins such as SARS and HIV-1. Additionally mimicyp lacks peptidyl-prolyl isomerase activity in contrast to human cyclophilins. Thus, this study suggests that cyclophilins, whether recruited from host cells (i.e. HIV-1 and SARS) or virally encoded (i.e. Mimivirus), are localized on viral surfaces for at least a subset of viruses.
| | The line below this paragraph, {{ABSTRACT_PUBMED_18342330}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18342330 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18342330}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Isomerase]] | | [[Category: Isomerase]] |
| [[Category: Mimivirus]] | | [[Category: Mimivirus]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:30:37 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:14:39 2008'' |
