1e8i: Difference between revisions

Revision as of 13:25, 21 February 2008

HUMAN CD69-TETRAGONAL 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

1E8I is a Single protein structure of sequence from Homo sapiens with as ligand. 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

Page seeded by OCA on Thu Feb 21 12:25:01 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1e8i.gif|left|200px]]<br />
+[[Image:1e8i.gif|left|200px]]<br /><applet load="1e8i" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1e8i" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1e8i, resolution 1.95&Aring;" />
 '''HUMAN CD69-TETRAGONAL FORM'''<br />
 ==Overview==
-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.
+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 Structure==
-E8I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E8I OCA].
+E8I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8I OCA].
 ==Reference==
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 [[Category: nkd]]
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