3G8L

Crystal structure of murine natural killer cell receptor, Ly49L4

Summary for 3G8L

• Entry DOI: 10.2210/pdb3g8l/pdb
• Related: 3G8K
• Descriptor: Lectin-related NK cell receptor LY49L1 (2 entities in total)
• Functional Keywords: natural killer cell receptor, ly49, receptor, immune system
• Biological source: Mus musculus (mouse)
• Total number of polymer chains: 4
• Total formula weight: 88280.50

Authors

Cho, S. (deposition date: 2009-02-12, release date: 2009-11-17, Last modification date: 2024-11-27)

Primary citation

Back, J.,Malchiodi, E.L.,Cho, S.,Scarpellino, L.,Schneider, P.,Kerzic, M.C.,Mariuzza, R.A.,Held, W.
Distinct conformations of Ly49 natural killer cell receptors mediate MHC class I recognition in trans and cis.
Immunity, 31:598-608, 2009

PubMed Abstract: Certain cell-surface receptors engage ligands expressed on juxtaposed cells and ligands on the same cell. The structural basis for trans versus cis binding is not known. Here, we showed that Ly49 natural killer (NK) cell receptors bound two MHC class I (MHC-I) molecules in trans when the two ligand-binding domains were backfolded onto the long stalk region. In contrast, dissociation of the ligand-binding domains from the stalk and their reorientation relative to the NK cell membrane allowed monovalent binding of MHC-I in cis. The distinct conformations (backfolded and extended) define the structural basis for cis-trans binding by Ly49 receptors and explain the divergent functional consequences of cis versus trans interactions. Further analyses identified specific stalk segments that were not required for MHC-I binding in trans but were essential for inhibitory receptor function. These data identify multiple distinct roles of stalk regions for receptor function.

PubMed: 19818651
DOI: 10.1016/j.immuni.2009.07.007

Experimental method

X-RAY DIFFRACTION (2.5 Å)