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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 Acta+Crystallogr+F+Struct+Biol+Commun
2015 ; 71
(Pt 6
): 697-701
Nephropedia Template TP
gab.com Text
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English Wikipedia
Expression, crystallization and X-ray diffraction analysis of a complex between
B7-H6, a tumor cell ligand for the natural cytotoxicity receptor NKp30, and an
inhibitory antibody
#MMPMID26057798
Xu X
; Li Y
; Gauthier L
; Chen Q
; Vivier E
; Mariuzza RA
Acta Crystallogr F Struct Biol Commun
2015[Jun]; 71
(Pt 6
): 697-701
PMID26057798
show ga
Natural killer (NK) cells are essential components of the innate immune response
to tumors and viral infections. In humans, the activating natural cytotoxicity
receptor NKp30 plays a major role in NK cell-mediated tumor cell lysis. NKp30
recognizes the cell-surface protein B7-H6, which is expressed on tumor, but not
healthy, cells. A mouse monoclonal antibody (17B1.3) against human B7-H6 has been
developed (Kd = 0.2 µM) to investigate NKp30-mediated NK cell activation and to
target tumors expressing B7-H6. Surprisingly, 17B1.3 blocks NK cell activation
without interfering with the binding of B7-H6 to NKp30. Understanding the
inhibitory mechanism of this antibody will require knowing the structure of
17B1.3 bound to B7-H6. The antigen-binding fragment (Fab) of 17B1.3 was expressed
by in vitro folding from bacterial inclusion bodies. The extracellular domain of
B7-H6 was produced by secretion from baculovirus-infected insect cells. Crystals
of the Fab 17B1.3-B7-H6 complex grown by macro-seeding diffracted to 2.5 Å
resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a
= 89.6, b = 138.0, c = 171.4 Å, ? = ? = ? = 90°. Comparison of the Fab
17B1.3-B7-H6 structure with the known NKp30-B7-H6 structure will elucidate the
inhibitory mechanism of 17B1.3.