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2L35

Structure of the DAP12-NKG2C transmembrane heterotrimer

Summary for 2L35
Entry DOI10.2210/pdb2l35/pdb
Related2HAC 2K4F 2L34
DescriptorDAP12-NKG2C_TM, TYRO protein tyrosine kinase-binding protein (2 entities in total)
Functional Keywordsimmunoreceptor, transmembrane assembly, dap12-nkg2c complex, protein binding
Biological sourceHomo sapiens (human)
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Cellular locationMembrane; Single-pass type I membrane protein: O43914
Total number of polymer chains2
Total formula weight9696.73
Authors
Call, M.E.,Wucherpfennig, K.W.,Chou, J.J. (deposition date: 2010-09-06, release date: 2010-11-03, Last modification date: 2024-11-20)
Primary citationCall, M.E.,Wucherpfennig, K.W.,Chou, J.J.
The structural basis for intramembrane assembly of an activating immunoreceptor complex.
Nat.Immunol., 11:1023-1029, 2010
Cited by
PubMed Abstract: Many receptors that activate cells of the immune system are multisubunit membrane protein complexes in which ligand recognition and signaling functions are contributed by separate protein modules. Receptors and signaling subunits assemble through contacts among basic and acidic residues in their transmembrane domains to form the functional complexes. Here we report the nuclear magnetic resonance (NMR) structure of the membrane-embedded, heterotrimeric assembly formed by association of the DAP12 signaling module with the natural killer (NK) cell-activating receptor NKG2C. The main intramembrane contact site is formed by a complex electrostatic network involving five hydrophilic transmembrane residues. Functional mutagenesis demonstrated that similar polar intramembrane motifs are also important for assembly of the NK cell-activating NKG2D-DAP10 complex and the T cell antigen receptor (TCR)-invariant signaling protein CD3 complex. This structural motif therefore lies at the core of the molecular organization of many activating immunoreceptors.
PubMed: 20890284
DOI: 10.1038/ni.1943
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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