1fm5
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CRYSTAL STRUCTURE OF HUMAN CD69
OverviewOverview
CD69 is a widely expressed type II transmembrane glycoprotein related to, the C-type animal lectins that exhibits regulated expression on a variety, of cells of the hematopoietic lineage, including neutrophils, monocytes, T, cells, B cells, natural killer (NK) cells, and platelets. Activation of T, lymphocytes results in the induced expression of CD69 at the cell surface., In addition, cross-linking of CD69 by specific antibodies leads to the, activation of cells bearing this receptor and to the induction of effector, functions. However, the physiological ligand of CD69 is unknown. We report, here the X-ray crystal structure of the extracellular C-type lectin-like, domain (CTLD) of human CD69 at 2.27 A resolution. Recombinant CD69 was, expressed in bacterial inclusion bodies and folded in vitro. The protein, which exists as a disulfide-linked homodimer on the cell surface, crystallizes as a symmetrical dimer, similar to those formed by the, related NK cell receptors Ly49A and CD94. The structure reveals, conservation of the C-type lectin-like fold, including preservation of the, two alpha-helical regions found in Ly49A and mannose-binding protein, (MBP). However, only one of the nine residues coordinated to Ca(2+) in MBP, is conserved in CD69 and no bound Ca(2+) is evident in the crystal, structure. Surprisingly, electron density suggestive of a puckered, six-membered ring was discovered at a site structurally analogous to the, ligand-binding sites of MBP and Ly49A. This sugar-like density may, represent, or mimic, part of the natural ligand recognized by CD69.
About this StructureAbout this Structure
1FM5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of human CD69: a C-type lectin-like activation marker of hematopoietic cells., Natarajan K, Sawicki MW, Margulies DH, Mariuzza RA, Biochemistry. 2000 Dec 5;39(48):14779-86. PMID:11101293
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