3CAD
Crystal structure of Natural Killer Cell Receptor, Ly49G
Summary for 3CAD
| Entry DOI | 10.2210/pdb3cad/pdb |
| Descriptor | Lectin-related NK cell receptor LY49G1 (2 entities in total) |
| Functional Keywords | ly49g, c-type lectin-like domain, natural killer receptor domain, unknown function |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 2 |
| Total formula weight | 29151.42 |
| Authors | |
| Primary citation | Deng, L.,Cho, S.,Malchiodi, E.L.,Kerzic, M.C.,Dam, J.,Mariuzza, R.A. Molecular Architecture of the Major Histocompatibility Complex Class I-binding Site of Ly49 Natural Killer Cell Receptors. J.Biol.Chem., 283:16840-16849, 2008 Cited by PubMed Abstract: Natural killer (NK) cells play a vital role in the detection and destruction of virally infected and tumor cells during innate immune responses. The highly polymorphic Ly49 family of NK receptors regulates NK cell function by sensing major histocompatibility complex class I (MHC-I) molecules on target cells. Despite the determination of two Ly49-MHC-I complex structures, the molecular features of Ly49 receptors that confer specificity for particular MHC-I alleles have not been identified. To understand the functional architecture of Ly49-binding sites, we determined the crystal structures of Ly49C and Ly49G and completed refinement of the Ly49C-H-2K(b) complex. This information, combined with mutational analysis of Ly49A, permitted a structure-based classification of Ly49s that we used to dissect the binding site into three distinct regions, each having different roles in MHC recognition. One region, located at the center of the binding site, has a similar structure across the Ly49 family and mediates conserved interactions with MHC-I that contribute most to binding. However, the preference of individual Ly49s for particular MHC-I molecules is governed by two regions that flank the central region and are structurally more variable. One of the flanking regions divides Ly49s into those that recognize both H-2D and H-2K versus only H-2D ligands, whereas the other discriminates among H-2D or H-2K alleles. The modular design of Ly49-binding sites provides a framework for predicting the MHC-binding specificity of Ly49s that have not been characterized experimentally. PubMed: 18426793DOI: 10.1074/jbc.M801526200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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