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J. Biol. Chem., Vol. 276, Issue 10, 7312-7319, March 9, 2001
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From the Department of Macromolecular Structure, Centro Nacional de
Biotecnología, Universidad Autónoma de Madrid, 28049 Madrid, Spain, 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 Ca2+ 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 The atomic coordinates and the structure factors (code 1E87 and 1E8I) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).
Crystal Structure of the C-type Lectin-like Domain from the Human
Hematopoietic Cell Receptor CD69*
, Instituto de Estudios de la Inmunidad
Humoral, Consejo Nacional de Investigaciones Científicas
y Técnicas-Universidad de Buenos Aires, Junín 956, 1113 Buenos Aires, Argentina, and § Servicio de
Inmunología, Hospital de la Princesa, Universidad
Autónoma de Madrid, 28006 Madrid, Spain
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.
*
This work was supported by the Spanish Dirección
General de Enseñanza Superior (PB96-0271) and Fundación
Antorchas, Argentina.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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