• Something wrong with this record ?

Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 23 Å resolution

P. Kolenko, D. Rozbeský, O. Vaněk, K. Bezouška, J. Hašek, J. Dohnálek

. 2011 ; 67 (Pt 12) : 1519-1523. [pub] 20111130

Language English Country Great Britain

Document type Journal Article, Research Support, Non-U.S. Gov't

Persistent link   https://www.medvik.cz/link/bmc12022072

The structure of the H107R variant of the extracellular domain of the mouse natural killer cell receptor NKR-P1A has been determined by X-ray diffraction at 2.3 Å resolution from a merohedrally twinned crystal. Unlike the structure of the wild-type receptor in space group I4(1)22 with a single chain per asymmetric unit, the crystals of the variant belonged to space group I4(1) with a dimer in the asymmetric unit. Different degrees of merohedral twinning were detected in five data sets collected from different crystals. The mutation does not have a significant impact on the overall structure, but led to the binding of an additional phosphate ion at the interface of the molecules.

References provided by Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc12022072
003      
CZ-PrNML
005      
20121206103152.0
007      
ta
008      
120806e20111130xxk f 000 0#eng||
009      
AR
024    7_
$a 10.1107/s1744309111046203 $2 doi
035    __
$a (PubMed)22139156
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a xxk
100    1_
$a Kolenko, Petr $7 xx0124748 $u Institute of Macromolecular Chemistry AS CR, vvi, Prague, Czech Republic. kolenko@imc.cas.cz
245    10
$a Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 23 Å resolution / $c P. Kolenko, D. Rozbeský, O. Vaněk, K. Bezouška, J. Hašek, J. Dohnálek
520    9_
$a The structure of the H107R variant of the extracellular domain of the mouse natural killer cell receptor NKR-P1A has been determined by X-ray diffraction at 2.3 Å resolution from a merohedrally twinned crystal. Unlike the structure of the wild-type receptor in space group I4(1)22 with a single chain per asymmetric unit, the crystals of the variant belonged to space group I4(1) with a dimer in the asymmetric unit. Different degrees of merohedral twinning were detected in five data sets collected from different crystals. The mutation does not have a significant impact on the overall structure, but led to the binding of an additional phosphate ion at the interface of the molecules.
650    _2
$a zvířata $7 D000818
650    _2
$a krystalografie rentgenová $7 D018360
650    _2
$a extracelulární prostor $x chemie $7 D005110
650    _2
$a myši $7 D051379
650    _2
$a molekulární modely $7 D008958
650    _2
$a mutace $7 D009154
650    _2
$a lektinové receptory NK-buněk - podrodina B $x chemie $x genetika $7 D055651
650    _2
$a kvarterní struktura proteinů $7 D020836
650    _2
$a terciární struktura proteinů $7 D017434
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Rozbeský, Daniel. $7 _AN068790
700    1_
$a Vaněk, Ondřej $7 xx0147860
700    1_
$a Bezouška, Karel, $d 1960- $7 jo2005273852
700    1_
$a Hašek, Jindřich, $d 1946- $7 mzk2006331646
700    1_
$a Dohnálek, Jan $7 xx0063750
773    0_
$w MED00179506 $t Acta crystallographica. Section F, Structural biology and crystallization communications $x 1744-3091 $g Roč. 67, č. Pt 12 (20111130), s. 1519-1523
856    41
$u https://pubmed.ncbi.nlm.nih.gov/22139156 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y m
990    __
$a 20120806 $b ABA008
991    __
$a 20121206103226 $b ABA008
999    __
$a ok $b bmc $g 943985 $s 779369
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2011 $b 67 $c Pt 12 $d 1519-1523 $e 20111130 $i 1744-3091 $m Acta crystallographica. Section F $n Acta Crystallogr Sect F Struct Biol Cryst Commun $x MED00179506
LZP    __
$a Pubmed-20120806/12/01/jt

Find record

Citation metrics

Archiving options