1e87
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HUMAN CD69-TRIGONAL FORM
OverviewOverview
CD69, one of the earliest specific antigens acquired during lymphoid, activation, acts as a signal-transducing receptor involved in cellular, activation events, including proliferation and induction of specific, genes. CD69 belongs to a family of receptors that modulate the immune, response and whose genes are clustered in the natural killer (NK) gene, complex. The extracellular portion of these receptors represent a, subfamily of C-type lectin-like domains (CTLDs), which are divergent from, true C-type lectins and are referred to as NK-cell domains (NKDs). We have, determined the three-dimensional structure of human CD69 NKD in two, different crystal forms. CD69 NKD adopts the canonical CTLD fold but lacks, the features involved in Ca(2+) and carbohydrate binding by C-type, lectins. CD69 NKD dimerizes noncovalently, both in solution and in, crystalline state. The dimer interface consists of a hydrophobic, loosely, packed core, surrounded by polar interactions, including an interdomain, beta sheet. The intersubunit core shows certain structural plasticity that, may facilitate conformational rearrangements for binding to ligands. The, surface equivalent to the binding site of other members of the CTLD, superfamily reveals a hydrophobic patch surrounded by conserved charged, residues that probably constitutes the CD69 ligand-binding site.
About this StructureAbout this Structure
1E87 is a Single protein structure of sequence from Homo sapiens with ZN and GOL as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the C-type lectin-like domain from the human hematopoietic cell receptor CD69., Llera AS, Viedma F, Sanchez-Madrid F, Tormo J, J Biol Chem. 2001 Mar 9;276(10):7312-9. Epub 2000 Oct 17. PMID:11036086
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