This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4lla

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 19:30, 25 December 2014

Crystal structure of D3D4 domain of the LILRB2 molecule

Structural highlights

4lla is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	4ll9
Gene:	LILRB2 (Homo sapiens)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[LIRB2_HUMAN] Receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C and HLA-G alleles. Involved in the down-regulation of the immune response and the development of tolerance. Competes with CD8A for binding to class I MHC antigens. Inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

Leukocyte immunoglobulin-like receptors (LILRs), also called CD85s, ILTs, or LIRs, are important mediators of immune activation and tolerance that contain tandem immunoglobulin (Ig)-like folds. There are 11 (in addition to two pseudogenes) LILRs in total, two with two Ig-like domains (D1D2) and the remaining nine with four Ig-like domains (D1D2D3D4). Thus far, the structural features of the D1D2 domains of LILR proteins are well defined, but no structures for the D3D4 domains have been reported. This is a very important field to be studied as it relates to the unknown functions of the D3D4 domains, as well as their relative orientation to the D1D2 domains on the cell surface. Here, we report the crystal structures of the D3D4 domains of both LILRB1 and LILRB2. The two Iglike domains of both LILRB1-D3D4 and LILRB2-D3D4 are arranged at an acute angle ( approximately 60 degrees ) to form a bent structure, resembling the structures of natural killer inhibitory receptors. Based on these two D3D4 domain structures and previously reported D1D2/HLA I complex structures, two alternative models of full-length (four Ig-like domains) LILR molecules bound to HLA I are proposed.

Crystal structures of the two membrane-proximal Ig-like domains (D3D4) of LILRB1/B2: alternative models for their involvement in peptide-HLA binding.,Nam G, Shi Y, Ryu M, Wang Q, Song H, Liu J, Yan J, Qi J, Gao GF Protein Cell. 2013 Aug 17. PMID:23955630^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Borges L, Hsu ML, Fanger N, Kubin M, Cosman D. A family of human lymphoid and myeloid Ig-like receptors, some of which bind to MHC class I molecules. J Immunol. 1997 Dec 1;159(11):5192-6. PMID:9548455
↑ Fanger NA, Cosman D, Peterson L, Braddy SC, Maliszewski CR, Borges L. The MHC class I binding proteins LIR-1 and LIR-2 inhibit Fc receptor-mediated signaling in monocytes. Eur J Immunol. 1998 Nov;28(11):3423-34. PMID:9842885
↑ Chang CC, Ciubotariu R, Manavalan JS, Yuan J, Colovai AI, Piazza F, Lederman S, Colonna M, Cortesini R, Dalla-Favera R, Suciu-Foca N. Tolerization of dendritic cells by T(S) cells: the crucial role of inhibitory receptors ILT3 and ILT4. Nat Immunol. 2002 Mar;3(3):237-43. Epub 2002 Jan 28. PMID:11875462 doi:10.1038/ni760
↑ Shiroishi M, Tsumoto K, Amano K, Shirakihara Y, Colonna M, Braud VM, Allan DS, Makadzange A, Rowland-Jones S, Willcox B, Jones EY, van der Merwe PA, Kumagai I, Maenaka K. Human inhibitory receptors Ig-like transcript 2 (ILT2) and ILT4 compete with CD8 for MHC class I binding and bind preferentially to HLA-G. Proc Natl Acad Sci U S A. 2003 Jul 22;100(15):8856-61. Epub 2003 Jul 9. PMID:12853576 doi:10.1073/pnas.1431057100
↑ Nam G, Shi Y, Ryu M, Wang Q, Song H, Liu J, Yan J, Qi J, Gao GF. Crystal structures of the two membrane-proximal Ig-like domains (D3D4) of LILRB1/B2: alternative models for their involvement in peptide-HLA binding. Protein Cell. 2013 Aug 17. PMID:23955630 doi:10.1007/s13238-013-3908-x

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4lla"

@@ Line 7: / Line 7: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lla OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lla RCSB], [http://www.ebi.ac.uk/pdbsum/4lla PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/LIRB2_HUMAN LIRB2_HUMAN]] Receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C and HLA-G alleles. Involved in the down-regulation of the immune response and the development of tolerance. Competes with CD8A for binding to class I MHC antigens. Inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions.<ref>PMID:9548455</ref> <ref>PMID:9842885</ref> <ref>PMID:11875462</ref> <ref>PMID:12853576</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4lla

From Proteopedia

Revision as of 19:30, 25 December 2014

Crystal structure of D3D4 domain of the LILRB2 molecule

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox