1998
DOI: 10.1107/s0907444997015229
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Expression, purification, crystallization and crystallographic characterization of the human MHC class I related protein MICA

Abstract: Crystals of the human MHC-encoded molecule MICA, a homologue of MHC class I proteins, have been grown in hanging-drop vapor-diffusion trials using ammonium sulfate as a precipitating agent with recombinant protein expressed in a baculovirus-based system. Cryo-preserved crystals of MICA belong to the cubic space group F4132 with lattice constants a = b = c = 260.7 A and diffract to a resolution limit of 3.0 A when cryo-preserved. These crystals do not diffract when handled conventionally.

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Cited by 13 publications
(7 citation statements)
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“…MIC-A and MIC-B contain α1, α2, and α3 MHC domains. Interestingly, none of these ligands are able to bind to the β-2 microglobulin to form the classical MHC class I heterodimeric complexes(Bauer et al , 1998). The α1 and α2 helices of NKG2D ligands lack critical residues that have been shown to interact with the antigenic epitopes that result in the narrowing and partial obstruction of peptide binding grove.…”
Section: Protein Structure and Affinity Of Murine Nkg2d Ligandsmentioning
confidence: 99%
“…MIC-A and MIC-B contain α1, α2, and α3 MHC domains. Interestingly, none of these ligands are able to bind to the β-2 microglobulin to form the classical MHC class I heterodimeric complexes(Bauer et al , 1998). The α1 and α2 helices of NKG2D ligands lack critical residues that have been shown to interact with the antigenic epitopes that result in the narrowing and partial obstruction of peptide binding grove.…”
Section: Protein Structure and Affinity Of Murine Nkg2d Ligandsmentioning
confidence: 99%
“…Thus, surface expression of MIC on transformed cells is proposed to mark nascent tumors for immune surveillance (6)(7)(8). MIC proteins share structural homology with MHC class I molecules but have no role in antigen presentation (19). The two closely related MICs MICA and MICB share 84% amino acid sequence identity in the ectodomain and are suggested to be derived from recent gene duplication events (20).…”
Section: Introductionmentioning
confidence: 99%
“…The mAb 6G6 was generated by immunization of mice with mouse LTK-MICA transfectants and recognizes an epitope on the ␣ 3 domain of MICA and MICB; this mAb is of the IgG1 isotype (V.G., unpublished data) (13). The polyclonal antiserum (provided by S. Bauer, Fred Hutchinson Cancer Research Center, Seattle) was raised in rabbits by immunization with soluble MICA protein lacking transmembrane and cytoplasmic tail sequences; the soluble protein was expressed in Drosophila Schneider cells and purified from culture supernatant as described (17). Surface expression of MIC molecules on cell lines and transfectants was detected by indirect immunofluorescence stainings using mAb 6G6 or the polyclonal antiserum, f luorochromeconjugated goat anti-mouse or anti-rabbit Ig, and a FACScan flow cytometer (Becton Dickinson).…”
Section: Methodsmentioning
confidence: 99%