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1p7q

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==Overview==
==Overview==
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Leukocyte immunoglobulin-like receptor 1 (LIR-1), an inhibitory receptor, expressed on monocytes, dendritic cells and lymphocytes, regulates, cellular function by binding a broad range of classical and nonclassical, major histocompatibility complex (MHC) class I molecules, and the human, cytomegalovirus MHC class I homolog UL18. Here we describe the 3.4-A, crystal structure of a complex between the LIR-1 D1D2 domains and the MHC, class I molecule HLA-A2. LIR-1 contacts the mostly conserved, beta(2)-microglobulin and alpha3 domains of HLA-A2. The LIR-1 binding site, comprises residues at the interdomain hinge, and a patch at the D1 tip., The structure shows how LIR-1 recognizes UL18 and diverse MHC class I, molecules, and indicates that a similar mode of MHC class I recognition is, used by other LIR family members.
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Leukocyte immunoglobulin-like receptor 1 (LIR-1), an inhibitory receptor expressed on monocytes, dendritic cells and lymphocytes, regulates cellular function by binding a broad range of classical and nonclassical major histocompatibility complex (MHC) class I molecules, and the human cytomegalovirus MHC class I homolog UL18. Here we describe the 3.4-A crystal structure of a complex between the LIR-1 D1D2 domains and the MHC class I molecule HLA-A2. LIR-1 contacts the mostly conserved beta(2)-microglobulin and alpha3 domains of HLA-A2. The LIR-1 binding site comprises residues at the interdomain hinge, and a patch at the D1 tip. The structure shows how LIR-1 recognizes UL18 and diverse MHC class I molecules, and indicates that a similar mode of MHC class I recognition is used by other LIR family members.
==Disease==
==Disease==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Bjorkman, P.J.]]
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[[Category: Bjorkman, P J.]]
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[[Category: Thomas, L.M.]]
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[[Category: Thomas, L M.]]
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[[Category: Willcox, B.E.]]
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[[Category: Willcox, B E.]]
[[Category: hla-a2/lir-1 complex]]
[[Category: hla-a2/lir-1 complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:39:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:11 2008''

Revision as of 12:26, 21 February 2008


1p7q, resolution 3.40Å

Drag the structure with the mouse to rotate

Crystal Structure of HLA-A2 Bound to LIR-1, a Host and Viral MHC Receptor

Contents

Overview

Leukocyte immunoglobulin-like receptor 1 (LIR-1), an inhibitory receptor expressed on monocytes, dendritic cells and lymphocytes, regulates cellular function by binding a broad range of classical and nonclassical major histocompatibility complex (MHC) class I molecules, and the human cytomegalovirus MHC class I homolog UL18. Here we describe the 3.4-A crystal structure of a complex between the LIR-1 D1D2 domains and the MHC class I molecule HLA-A2. LIR-1 contacts the mostly conserved beta(2)-microglobulin and alpha3 domains of HLA-A2. The LIR-1 binding site comprises residues at the interdomain hinge, and a patch at the D1 tip. The structure shows how LIR-1 recognizes UL18 and diverse MHC class I molecules, and indicates that a similar mode of MHC class I recognition is used by other LIR family members.

Disease

Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142800], Ankylosing spondylitis, susceptibility to, 1 OMIM:[142800], Hypoproteinemia, hypercatabolic OMIM:[109700], Stevens-Johnson syndrome, susceptibility to OMIM:[142800]

About this Structure

1P7Q is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of HLA-A2 bound to LIR-1, a host and viral major histocompatibility complex receptor., Willcox BE, Thomas LM, Bjorkman PJ, Nat Immunol. 2003 Sep;4(9):913-9. Epub 2003 Aug 3. PMID:12897781

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