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Statements

Subject Item
n2:RIV%2F60076658%3A12310%2F13%3A43883864%21RIV14-MSM-12310___
rdf:type
n7:Vysledek skos:Concept
dcterms:description
NKR-P1C is an activating immune receptor expressed on the surface of mouse natural killer cells. It has been widely used as a marker for NK cell identification in different mice strains. Recently we solved a crystal structure of the C-type lectin-like domain of a homologous protein, NKR-P1A, using X-ray crystallography and also described the strategy for rapid characterization of the protein conformation in solution. This procedure utilized chemical cross-linking, hydrogen/deuterium exchange, and molecular modeling. It was found that the solution structure differs from the crystal structure in the conformation of the loop region. The loop, detached from the protein compact core in the crystal structure, is closely attached to the core of the protein in solution. Here we present and interpret the solution structure of the C-type lectin-like domain of NKR-P1C using chemical cross-linking and molecular modeling. The validation of the model and conformation of the loop region in NKR-P1C were addressed using ion-mobility mass spectrometry. NKR-P1C is an activating immune receptor expressed on the surface of mouse natural killer cells. It has been widely used as a marker for NK cell identification in different mice strains. Recently we solved a crystal structure of the C-type lectin-like domain of a homologous protein, NKR-P1A, using X-ray crystallography and also described the strategy for rapid characterization of the protein conformation in solution. This procedure utilized chemical cross-linking, hydrogen/deuterium exchange, and molecular modeling. It was found that the solution structure differs from the crystal structure in the conformation of the loop region. The loop, detached from the protein compact core in the crystal structure, is closely attached to the core of the protein in solution. Here we present and interpret the solution structure of the C-type lectin-like domain of NKR-P1C using chemical cross-linking and molecular modeling. The validation of the model and conformation of the loop region in NKR-P1C were addressed using ion-mobility mass spectrometry.
dcterms:title
Structural model of lymphocyte receptor NKR-P1C revealed bymass spectrometry and molecular modelling Structural model of lymphocyte receptor NKR-P1C revealed bymass spectrometry and molecular modelling
skos:prefLabel
Structural model of lymphocyte receptor NKR-P1C revealed bymass spectrometry and molecular modelling Structural model of lymphocyte receptor NKR-P1C revealed bymass spectrometry and molecular modelling
skos:notation
RIV/60076658:12310/13:43883864!RIV14-MSM-12310___
n7:predkladatel
n12:orjk%3A12310
n3:aktivita
n5:Z n5:S
n3:aktivity
S, Z(MSM6007665808)
n3:cisloPeriodika
3
n3:dodaniDat
n9:2014
n3:domaciTvurceVysledku
n16:6326633 n16:8246157
n3:druhVysledku
n8:J
n3:duvernostUdaju
n18:S
n3:entitaPredkladatele
n20:predkladatel
n3:idSjednocenehoVysledku
108361
n3:idVysledku
RIV/60076658:12310/13:43883864
n3:jazykVysledku
n13:eng
n3:klicovaSlova
lymphocyte receptor, molecular modeling, solution structure, chemical cross-linking, hydrogen/deuterium exchange
n3:klicoveSlovo
n4:hydrogen%2Fdeuterium%20exchange n4:lymphocyte%20receptor n4:chemical%20cross-linking n4:solution%20structure n4:molecular%20modeling
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[8AF10A661332]
n3:nazevZdroje
Analytical chemistry
n3:obor
n11:CE
n3:pocetDomacichTvurcuVysledku
2
n3:pocetTvurcuVysledku
7
n3:rokUplatneniVysledku
n9:2013
n3:svazekPeriodika
85
n3:tvurceVysledku
Novák, Petr Rozbeský, Daniel Man, Petr Robinson, Carol V Sovová, Žofie Marcoux, Julien Ettrich, Ruediger Horst
n3:wos
000314676100051
n3:zamer
n14:MSM6007665808
s:issn
0003-2700
s:numberOfPages
8
n19:doi
10.1021/ac302860m
n17:organizacniJednotka
12310