3bdw

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(New page: 200px<br /><applet load="3bdw" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bdw, resolution 2.500&Aring;" /> '''Human CD94/NKG2A'''...)
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==Overview==
==Overview==
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The CD94-NKG2 receptor family that regulates NK and T cells is unique, among the lectin-like receptors encoded within the natural killer cell, complex. The function of the CD94-NKG2 receptors is dictated by the, pairing of the invariant CD94 polypeptide with specific NKG2 isoforms to, form a family of functionally distinct heterodimeric receptors. However, the structural basis for this selective pairing and how they interact with, their ligand, HLA-E, is unknown. We describe the 2.5 A resolution crystal, structure of CD94-NKG2A in which the mode of dimerization contrasts with, that of other homodimeric NK receptors. Despite structural homology, between the CD94 and NKG2A subunits, the dimer interface is asymmetric, thereby providing a structural basis for the preferred heterodimeric, assembly. Structure-based sequence comparisons of other CD94-NKG2 family, members, combined with extensive mutagenesis studies on HLA-E and, CD94-NKG2A, allows a model of the interaction between CD94-NKG2A and HLA-E, to be established, in which the invariant CD94 chain plays a more dominant, role in interacting with HLA-E in comparison to the variable NKG2 chain.
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The CD94-NKG2 receptor family that regulates NK and T cells is unique among the lectin-like receptors encoded within the natural killer cell complex. The function of the CD94-NKG2 receptors is dictated by the pairing of the invariant CD94 polypeptide with specific NKG2 isoforms to form a family of functionally distinct heterodimeric receptors. However, the structural basis for this selective pairing and how they interact with their ligand, HLA-E, is unknown. We describe the 2.5 A resolution crystal structure of CD94-NKG2A in which the mode of dimerization contrasts with that of other homodimeric NK receptors. Despite structural homology between the CD94 and NKG2A subunits, the dimer interface is asymmetric, thereby providing a structural basis for the preferred heterodimeric assembly. Structure-based sequence comparisons of other CD94-NKG2 family members, combined with extensive mutagenesis studies on HLA-E and CD94-NKG2A, allows a model of the interaction between CD94-NKG2A and HLA-E to be established, in which the invariant CD94 chain plays a more dominant role in interacting with HLA-E in comparison to the variable NKG2 chain.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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The Heterodimeric Assembly of the CD94-NKG2 Receptor Family and Implications for Human Leukocyte Antigen-E Recognition., Sullivan LC, Clements CS, Beddoe T, Johnson D, Hoare HL, Lin J, Huyton T, Hopkins EJ, Reid HH, Wilce MC, Kabat J, Borrego F, Coligan JE, Rossjohn J, Brooks AG, Immunity. 2007 Dec;27(6):900-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18083576 18083576]
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The heterodimeric assembly of the CD94-NKG2 receptor family and implications for human leukocyte antigen-E recognition., Sullivan LC, Clements CS, Beddoe T, Johnson D, Hoare HL, Lin J, Huyton T, Hopkins EJ, Reid HH, Wilce MC, Kabat J, Borrego F, Coligan JE, Rossjohn J, Brooks AG, Immunity. 2007 Dec;27(6):900-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18083576 18083576]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Clements, C.S.]]
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[[Category: Clements, C S.]]
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[[Category: Sullivan, L.C.]]
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[[Category: Sullivan, L C.]]
[[Category: alternative splicing]]
[[Category: alternative splicing]]
[[Category: glycoprotein]]
[[Category: glycoprotein]]
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[[Category: transmembrane]]
[[Category: transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:20:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:05:05 2008''

Revision as of 17:05, 21 February 2008


3bdw, resolution 2.500Å

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Human CD94/NKG2A

Overview

The CD94-NKG2 receptor family that regulates NK and T cells is unique among the lectin-like receptors encoded within the natural killer cell complex. The function of the CD94-NKG2 receptors is dictated by the pairing of the invariant CD94 polypeptide with specific NKG2 isoforms to form a family of functionally distinct heterodimeric receptors. However, the structural basis for this selective pairing and how they interact with their ligand, HLA-E, is unknown. We describe the 2.5 A resolution crystal structure of CD94-NKG2A in which the mode of dimerization contrasts with that of other homodimeric NK receptors. Despite structural homology between the CD94 and NKG2A subunits, the dimer interface is asymmetric, thereby providing a structural basis for the preferred heterodimeric assembly. Structure-based sequence comparisons of other CD94-NKG2 family members, combined with extensive mutagenesis studies on HLA-E and CD94-NKG2A, allows a model of the interaction between CD94-NKG2A and HLA-E to be established, in which the invariant CD94 chain plays a more dominant role in interacting with HLA-E in comparison to the variable NKG2 chain.

About this Structure

3BDW is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The heterodimeric assembly of the CD94-NKG2 receptor family and implications for human leukocyte antigen-E recognition., Sullivan LC, Clements CS, Beddoe T, Johnson D, Hoare HL, Lin J, Huyton T, Hopkins EJ, Reid HH, Wilce MC, Kabat J, Borrego F, Coligan JE, Rossjohn J, Brooks AG, Immunity. 2007 Dec;27(6):900-11. PMID:18083576

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