Lack of involvement of strand s1′A of the viral serpin CrmA in anti-apoptotic or caspase-inhibitory functions

Simonović, Miljan; Denault, Jean Bernard; Salvesen, Guy S.; Volz, Karl; Gettins, Peter G.W.

doi:10.1016/j.abb.2005.05.018

Cited by 2 publications

(2 citation statements)

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“…There were many new insights into the structure and biochemistry of serpins with extra‐inhibitory and cross‐class inhibitory functions. Guy Salvesen (The Burnham Institute, USA) presented a study of cross‐class inhibition of caspases by viral serpins and the control of cell death [20]. Continuing on the theme of cross‐class inhibition, Sheena McGowan (Monash University, Australia) presented several X‐ray crystal structures of the myeloid and erythroid nuclear termination stage specific protein (MENT), with these data revealing a possible mechanism by which this unusual nuclear cysteine protease inhibitor can interact with DNA and chromatin [3,21].…”

Section: Meeting Reportmentioning

confidence: 99%

Serpins 2005 – fun between the β‐sheets

Whisstock

Bottomley²,

Bird³

et al. 2005

The FEBS Journal

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Serpins are the largest family of protease inhibitors and are fundamental for the control of proteolysis in multicellular eukaryotes. Most eukaryote serpins inhibit serine or cysteine proteases, however, noninhibitory members have been identified that perform diverse functions in processes such as hormone delivery and tumour metastasis. More recently inhibitory serpins have been identified in prokaryotes and unicellular eukaryotes, nevertheless, the precise molecular targets of these molecules remains to be identified. The serpin mechanism of protease inhibition is unusual and involves a major conformational rearrangement of the molecule concomitant with a distortion of the target protease. As a result of this requirement, serpins are susceptible to mutations that result in polymerization and conformational diseases such as the human serpinopathies. This review reports on recent major discoveries in the serpin field, based upon presentations made at the 4th International Symposium on Serpin Structure, Function and Biology (Cairns, Australia).

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Section: Meeting Reportmentioning

confidence: 99%

Serpins 2005 – fun between the β‐sheets

Whisstock

Bottomley²,

Bird³

et al. 2005

The FEBS Journal

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show abstract

“…Expressing viral proteins that inhibit apoptosis is one mechanism that poxviruses use to evade the host innate immune response at the cellular level. Studies of the X-ray crystal structure of CrmA showed that it has a structure similar to that of other serpins, even though there is very little primary sequence similarity to any one cellular serpin (153,154). Orthopoxviruses encode three serpins, SPI-1, SPI-2/CrmA, and SPI-3.…”

Section: Proteomics and Virus-host Protein Interaction 739mentioning

confidence: 99%

Poxvirus Proteomics and Virus-Host Protein Interactions

Vliet

Mohamed

Zhang

et al. 2009

Microbiol Mol Biol Rev

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SUMMARY Studies of the functional proteins encoded by the poxvirus genome provide information about the composition of the virus as well as individual virus-virus protein and virus-host protein interactions, which provides insight into viral pathogenesis and drug discovery. Widely used proteomic techniques to identify and characterize specific protein-protein interactions include yeast two-hybrid studies and coimmunoprecipitations. Recently, various mass spectrometry techniques have been employed to identify viral protein components of larger complexes. These methods, combined with structural studies, can provide new information about the putative functions of viral proteins as well as insights into virus-host interaction dynamics. For viral proteins of unknown function, identification of either viral or host binding partners provides clues about their putative function. In this review, we discuss poxvirus proteomics, including the use of proteomic methodologies to identify viral components and virus-host protein interactions. High-throughput global protein expression studies using protein chip technology as well as new methods for validating putative protein-protein interactions are also discussed.

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Lack of involvement of strand s1′A of the viral serpin CrmA in anti-apoptotic or caspase-inhibitory functions

Cited by 2 publications

References 32 publications

Serpins 2005 – fun between the β‐sheets

Serpins 2005 – fun between the β‐sheets

Poxvirus Proteomics and Virus-Host Protein Interactions

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