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Statements

Subject Item
n2:RIV%2F60461373%3A22330%2F04%3A00012809%21RIV%2F2005%2FMSM%2F223305%2FN
rdf:type
skos:Concept n18:Vysledek
dcterms:description
Mason-Pfizer monkey virus assembles immature capsids in the cytoplasm and the temporal and spatial regulation of the maturation is critical, since the PR is not activated until immature capsids reach the cell membrane. Several evidences for a regulation of the activity of retroviral proteases by reversible oxidative modification of the cysteine residues were reported1,2. The structural and functional analysis of a mutant of M-PMV PR, in which two cysteine residues (Cys7, Cys106) were replaced by alanines confirmed, that this mutation decreases the stability, the proteolytic activity of PR, and the propensity of the monomers to form dimers3. Here we present results of a high resolution NMR structure of the inactive mutant (D26N) of the 12 kDa form of M-PMV PR with preserved cysteine residues. The data together with a biochemical characterization, MALDI-TOF analysis revealed the formation of an intramolecular disulphide bridge, which helps to stabilize the monomeric scaffold, and moves the chemical eq Mason-Pfizer monkey virus assembles immature capsids in the cytoplasm and the temporal and spatial regulation of the maturation is critical, since the PR is not activated until immature capsids reach the cell membrane. Several evidences for a regulation of the activity of retroviral proteases by reversible oxidative modification of the cysteine residues were reported1,2. The structural and functional analysis of a mutant of M-PMV PR, in which two cysteine residues (Cys7, Cys106) were replaced by alanines confirmed, that this mutation decreases the stability, the proteolytic activity of PR, and the propensity of the monomers to form dimers3. Here we present results of a high resolution NMR structure of the inactive mutant (D26N) of the 12 kDa form of M-PMV PR with preserved cysteine residues. The data together with a biochemical characterization, MALDI-TOF analysis revealed the formation of an intramolecular disulphide bridge, which helps to stabilize the monomeric scaffold, and moves the chemical eq vliv cysteinových zbytků na aktivitu proteasy Mason Pfizerova opičího viru
dcterms:title
vliv cysteinových zbytků na aktivitu proteasy Mason Pfizerova opičího viru INFLUENCE OF CYSTEINE RESIDUES ON THE ACTIVITY OF THE PROTEASE OF MASON-PFIZER MONKEY VIRUS. INFLUENCE OF CYSTEINE RESIDUES ON THE ACTIVITY OF THE PROTEASE OF MASON-PFIZER MONKEY VIRUS.
skos:prefLabel
vliv cysteinových zbytků na aktivitu proteasy Mason Pfizerova opičího viru INFLUENCE OF CYSTEINE RESIDUES ON THE ACTIVITY OF THE PROTEASE OF MASON-PFIZER MONKEY VIRUS. INFLUENCE OF CYSTEINE RESIDUES ON THE ACTIVITY OF THE PROTEASE OF MASON-PFIZER MONKEY VIRUS.
skos:notation
RIV/60461373:22330/04:00012809!RIV/2005/MSM/223305/N
n3:strany
76
n3:aktivita
n15:P
n3:aktivity
P(LN00A079)
n3:dodaniDat
n10:2005
n3:domaciTvurceVysledku
n6:9372040 n6:4866754 n6:6998798
n3:druhVysledku
n20:D
n3:duvernostUdaju
n9:S
n3:entitaPredkladatele
n21:predkladatel
n3:idSjednocenehoVysledku
567848
n3:idVysledku
RIV/60461373:22330/04:00012809
n3:jazykVysledku
n19:eng
n3:klicovaSlova
cysteine residues;protease
n3:klicoveSlovo
n16:cysteine%20residues n16:protease
n3:kontrolniKodProRIV
[4626669A6B5D]
n3:mistoKonaniAkce
Praha
n3:mistoVydani
Praha
n3:nazevZdroje
The Retrovirus Assembly meeting
n3:obor
n4:EE
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
5
n3:projekt
n17:LN00A079
n3:rokUplatneniVysledku
n10:2004
n3:tvurceVysledku
Pichová, Iva Hrabal, Richard Bauerová, Helena Ruml, Tomáš Svatoš, Aleš
n3:typAkce
n7:EUR
n3:zahajeniAkce
2004-01-01+01:00
s:numberOfPages
1
n14:hasPublisher
JPM Tisk s. r. o.
n8:isbn
80-86313-13-1
n11:organizacniJednotka
22330