First Molecular Graphics and Modelling Society Electronic Conference

Hardy, Barry; Doughty, Stephen W.; Parretti, Martin F.; Richards, W. Graham; Tennison, Jeni

doi:10.1016/s1093-3263(97)81619-1

Cited by 3 publications

(1 citation statement)

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“…The IRp60 homology model consisted of 104 total residues. The figures were prepared with Molscript [18], Render 3D [19] and Pymol (http://pymol.sourceforge.net/).…”

Section: Sequence Alignment and Construction Of The Irp60 Homology Modelmentioning

confidence: 99%

Molecular analysis and solution structure from small-angle X-ray scattering of the human natural killer inhibitory receptor IRp60 (CD300a)

Dimasi

Roessle

Morán

et al. 2007

International Journal of Biological Macromolecules

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“…The IRp60 homology model consisted of 104 total residues. The figures were prepared with Molscript [18], Render 3D [19] and Pymol (http://pymol.sourceforge.net/).…”

Section: Sequence Alignment and Construction Of The Irp60 Homology Modelmentioning

confidence: 99%

Molecular analysis and solution structure from small-angle X-ray scattering of the human natural killer inhibitory receptor IRp60 (CD300a)

Dimasi

Roessle

Morán

et al. 2007

International Journal of Biological Macromolecules

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(William) Graham Richards

Howard

Grant

2003

Molecular Physics

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Critical Residues at the Ly49 Natural Killer Receptor’s Homodimer Interface Determine Functional Recognition of m157, a Mouse Cytomegalovirus MHC Class I-Like Protein

Kielczewska

Kim

Lanier

et al. 2007

The Journal of Immunology

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NK cell function is regulated by Ly49 receptors in mice and killer cell Ig-like receptors in humans. Although inhibitory Ly49 and killer cell Ig-like receptors predominantly ligate classical MHC class I molecules, recent studies suggest that their activating counterparts recognize infection. The quintessential example is resistance to the mouse CMV in C57BL/6 mice, which depends on the functional recognition of m157, a mouse CMV-encoded MHC class I-like molecule, by Ly49H, an activating NK cell receptor. We have taken advantage of the natural variation in closely related members of the Ly49C-like receptors and the availability of Ly49 crystal structures to understand the molecular determinants of the Ly49H-m157 interaction and to identify amino acid residues discriminating between m157 binding and nonbinding receptors. Using a site-directed mutagenesis approach, we have targeted residues conserved in receptors binding to m157 (Ly49H and Ly49I129) but different from receptors lacking m157 recognition (Ly49C, Ly49IB6, and Ly49U). Wild-type and mutant receptors were transfected into reporter cells, and physical binding as well as functional activation by m157 was studied. Our findings suggested that the Ly49 MHC class I contact “site 2,” I226, may not be involved in m157 binding. In contrast, residue Y146 and G151, mapping at the receptor homodimer interface, are likely critical for functional recognition of the m157 glycoprotein. Our combined functional and three-dimensional modeling approach suggested that the architecture of the Ly49H dimer is crucial to accessing m157, but not MHC class I. These results link Ly49 homodimerization variability to the direct recognition of pathogen products.

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First Molecular Graphics and Modelling Society Electronic Conference

Cited by 3 publications

References 0 publications

Molecular analysis and solution structure from small-angle X-ray scattering of the human natural killer inhibitory receptor IRp60 (CD300a)

Molecular analysis and solution structure from small-angle X-ray scattering of the human natural killer inhibitory receptor IRp60 (CD300a)

(William) Graham Richards

Critical Residues at the Ly49 Natural Killer Receptor’s Homodimer Interface Determine Functional Recognition of m157, a Mouse Cytomegalovirus MHC Class I-Like Protein

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