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Statements

Subject Item
n2:RIV%2F67179843%3A_____%2F11%3A00371075%21RIV12-AV0-67179843
rdf:type
skos:Concept n14:Vysledek
dcterms:description
Receptor proteins at the cell surface regulate the ability of natural killer cells to recognize and kill a variety of aberrant target cells. The structural features determining the function of natural killer receptor proteins 1 (NKR-P1s) are largely unknown. In the present work, refined homology models are generated for the C-type lectin-like extracellular domains of rat NKR-P1A and NKR-P1B, mouse NKR-P1A, NKR-P1C, NKR-P1F, and NKR-P1G, and human NKR-P1 receptors. Experimental data on secondary structure, tertiary interactions, and thermal transitions are acquired for four of the proteins using Raman and infrared spectroscopy. The experimental and modeling results are in agreement with respect to the overall structures of the NKR-P1 receptor domains, while suggesting functionally significant local differences among species and isoforms. Two sequence regions that are conserved in all analyzed NKR-P1 receptors do not correspond to conserved structural elements as might be expected, but are represented by loop regions, one of which is arranged differently in the constructed models. This region displays high flexibility but is anchored by conserved sequences, suggesting that its position relative to the rest of the domain might be variable. This loop may contribute to ligand-binding specificity via a coupled conformational transition. Receptor proteins at the cell surface regulate the ability of natural killer cells to recognize and kill a variety of aberrant target cells. The structural features determining the function of natural killer receptor proteins 1 (NKR-P1s) are largely unknown. In the present work, refined homology models are generated for the C-type lectin-like extracellular domains of rat NKR-P1A and NKR-P1B, mouse NKR-P1A, NKR-P1C, NKR-P1F, and NKR-P1G, and human NKR-P1 receptors. Experimental data on secondary structure, tertiary interactions, and thermal transitions are acquired for four of the proteins using Raman and infrared spectroscopy. The experimental and modeling results are in agreement with respect to the overall structures of the NKR-P1 receptor domains, while suggesting functionally significant local differences among species and isoforms. Two sequence regions that are conserved in all analyzed NKR-P1 receptors do not correspond to conserved structural elements as might be expected, but are represented by loop regions, one of which is arranged differently in the constructed models. This region displays high flexibility but is anchored by conserved sequences, suggesting that its position relative to the rest of the domain might be variable. This loop may contribute to ligand-binding specificity via a coupled conformational transition.
dcterms:title
Structural analysis of natural killer cell receptor protein 1 (NKR-P1) extracellular domains suggests a conserved long loop region involved in ligand specificity Structural analysis of natural killer cell receptor protein 1 (NKR-P1) extracellular domains suggests a conserved long loop region involved in ligand specificity
skos:prefLabel
Structural analysis of natural killer cell receptor protein 1 (NKR-P1) extracellular domains suggests a conserved long loop region involved in ligand specificity Structural analysis of natural killer cell receptor protein 1 (NKR-P1) extracellular domains suggests a conserved long loop region involved in ligand specificity
skos:notation
RIV/67179843:_____/11:00371075!RIV12-AV0-67179843
n14:predkladatel
n15:ico%3A67179843
n3:aktivita
n10:Z n10:S n10:P
n3:aktivity
P(1M0505), P(KJB101120805), P(LC06010), S, Z(AV0Z50200510), Z(AV0Z60870520), Z(MSM0021620808), Z(MSM0021620835), Z(MSM6007665808)
n3:cisloPeriodika
6
n3:dodaniDat
n6:2012
n3:domaciTvurceVysledku
n19:6326633 n19:8246157
n3:druhVysledku
n18:J
n3:duvernostUdaju
n4:S
n3:entitaPredkladatele
n17:predkladatel
n3:idSjednocenehoVysledku
232716
n3:idVysledku
RIV/67179843:_____/11:00371075
n3:jazykVysledku
n12:eng
n3:klicovaSlova
cladogram; differential scanning calorimetry; FTIR; molecular dynamics; raman spectroscopy; RMSF; thermal dynamics; topology; two-dimensional correlation analysis
n3:klicoveSlovo
n7:cladogram n7:molecular%20dynamics n7:RMSF n7:thermal%20dynamics n7:raman%20spectroscopy n7:two-dimensional%20correlation%20analysis n7:differential%20scanning%20calorimetry n7:FTIR n7:topology
n3:kodStatuVydavatele
CZ - Česká republika
n3:kontrolniKodProRIV
[20A5522572BF]
n3:nazevZdroje
Journal of Molecular Modeling
n3:obor
n20:CE
n3:pocetDomacichTvurcuVysledku
2
n3:pocetTvurcuVysledku
8
n3:projekt
n8:LC06010 n8:1M0505 n8:KJB101120805
n3:rokUplatneniVysledku
n6:2011
n3:svazekPeriodika
17
n3:tvurceVysledku
Vaněk, Ondřej Sovová, Žofie Ettrich, Rüdiger Hofbauerová, Kateřina Rozbeský, Daniel Kopecký, V. Pazderka, T. Bezouška, K.
n3:wos
000291041800014
n3:zamer
n5:MSM0021620808 n5:MSM0021620835 n5:AV0Z50200510 n5:MSM6007665808 n5:AV0Z60870520
s:issn
1610-2940
s:numberOfPages
18
n13:doi
10.1007/s00894-010-0837-y