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4JO8

Crystal structure of the activating Ly49H receptor in complex with m157 (G1F strain)

Summary for 4JO8
Entry DOI10.2210/pdb4jo8/pdb
DescriptorM157, Killer cell lectin-like receptor 8, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
Functional Keywordsc-type lectin-like domain, natural killer receptor, viral immunoevasin, immune system-viral protein complex, immune system/viral protein
Biological sourceMurid herpesvirus 1 (MuHV-1)
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Cellular locationMembrane; Single-pass type II membrane protein: Q60682
Total number of polymer chains2
Total formula weight49299.14
Authors
Primary citationBerry, R.,Ng, N.,Saunders, P.M.,Vivian, J.P.,Lin, J.,Deuss, F.A.,Corbett, A.J.,Forbes, C.A.,Widjaja, J.M.,Sullivan, L.C.,McAlister, A.D.,Perugini, M.A.,Call, M.J.,Scalzo, A.A.,Degli-Esposti, M.A.,Coudert, J.D.,Beddoe, T.,Brooks, A.G.,Rossjohn, J.
Targeting of a natural killer cell receptor family by a viral immunoevasin
Nat.Immunol., 14:699-705, 2013
Cited by
PubMed Abstract: Activating and inhibitory receptors on natural killer (NK) cells have a crucial role in innate immunity, although the basis of the engagement of activating NK cell receptors is unclear. The activating receptor Ly49H confers resistance to infection with murine cytomegalovirus by binding to the 'immunoevasin' m157. We found that m157 bound to the helical stalk of Ly49H, whereby two m157 monomers engaged the Ly49H dimer. The helical stalks of Ly49H lay centrally across the m157 platform, whereas its lectin domain was not required for recognition. Instead, m157 targeted an 'aromatic peg motif' present in stalks of both activating and inhibitory receptors of the Ly49 family, and substitution of this motif abrogated binding. Furthermore, ligation of m157 to Ly49H or Ly49C resulted in intracellular signaling. Accordingly, m157 has evolved to 'tackle the legs' of a family of NK cell receptors.
PubMed: 23666294
DOI: 10.1038/ni.2605
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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