Structural model of lymphocyte receptor NKR-P1C revealed bymass spectrometry and molecular modelling

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F13%3A43883864" target="_blank" >RIV/60076658:12310/13:43883864 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1021/ac302860m" target="_blank" >http://dx.doi.org/10.1021/ac302860m</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/ac302860m" target="_blank" >10.1021/ac302860m</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Structural model of lymphocyte receptor NKR-P1C revealed bymass spectrometry and molecular modelling

Popis výsledku v původním jazyce

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 insolution. 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 we

Název v anglickém jazyce

Structural model of lymphocyte receptor NKR-P1C revealed bymass spectrometry and molecular modelling

Popis výsledku anglicky

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 insolution. 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 we

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

—

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2013

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Analytical chemistry

ISSN

0003-2700

e-ISSN

—

Svazek periodika

85

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

8

Strana od-do

1597-1604

Kód UT WoS článku

000314676100051

EID výsledku v databázi Scopus

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