2d3v: Difference between revisions

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[[Image:2d3v.gif|left|200px]]
{{Seed}}
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{{STRUCTURE_2d3v|  PDB=2d3v  |  SCENE=  }}  
{{STRUCTURE_2d3v|  PDB=2d3v  |  SCENE=  }}  


'''Crystal Structure of Leukocyte Ig-like Receptor A5 (LILRA5/LIR9/ILT11)'''
===Crystal Structure of Leukocyte Ig-like Receptor A5 (LILRA5/LIR9/ILT11)===




==Overview==
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Human leukocyte Ig-like receptor B1 (LILRB1) and B2 (LILRB2) belong to "Group 1" receptors and recognize a broad range of major histocompatibility complex class I molecules (MHCIs). In contrast, "Group 2" receptors show low similarity with LILRB1/B2, and their ligands remain to be identified. To date, the structural and functional characteristics of Group 2 LILRs are poorly understood. Here we report the crystal structure of the extracellular domain of LILRA5, which is an activating Group 2 LILR expressed on monocytes and neutrophils. Unexpectedly, the structure showed large changes in structural conformation and charge distribution in the region corresponding to the MHCI binding site of LILRB1/B2, which are also distinct from killer cell Ig-like receptors and Fc alpha receptors. These changes probably confer the structural hindrance for the MHCI binding, and their key amino acid substitutions are well conserved in Group 2 LILRs. Consistently, the surface plasmon resonance and flow cytometric analyses demonstrated that LILRA5 exhibited no affinities to all tested MHCIs. These results raised the possibility that LILRA5 as well as Group 2 LILRs do not play a role in any MHCI recognition but could possibly bind to non-MHCI ligand(s) on the target cells to provide a novel immune regulation mechanism.
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{{ABSTRACT_PUBMED_16675463}}


==About this Structure==
==About this Structure==
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[[Category: Shiroishi, M.]]
[[Category: Shiroishi, M.]]
[[Category: Immunoglobulin-like fold]]
[[Category: Immunoglobulin-like fold]]
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