1e87: Difference between revisions
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[[Image:1e87.gif|left|200px]] | [[Image:1e87.gif|left|200px]] | ||
'''HUMAN CD69-TRIGONAL FORM''' | {{Structure | ||
|PDB= 1e87 |SIZE=350|CAPTION= <scene name='initialview01'>1e87</scene>, resolution 1.50Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''HUMAN CD69-TRIGONAL FORM''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1E87 is a [ | 1E87 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E87 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11036086 11036086] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nkd]] | [[Category: nkd]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:51:24 2008'' | ||
Revision as of 11:51, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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