2f74

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{{STRUCTURE_2f74| PDB=2f74 | SCENE= }}
{{STRUCTURE_2f74| PDB=2f74 | SCENE= }}
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'''Murine MHC class I H-2Db in complex with human b2-microglobulin and LCMV-derived immunodminant peptide gp33'''
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===Murine MHC class I H-2Db in complex with human b2-microglobulin and LCMV-derived immunodminant peptide gp33===
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==Overview==
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beta(2)-Microglobulin (beta(2)m) is non-covalently linked to the major histocompatibility complex (MHC) class I heavy chain and interacts with CD8 and Ly49 receptors. Murine MHC class I heavy chains can bind human beta(2)m (hbeta(2)m) and peptide, and such hybrid molecules are often used in structural and functional studies. The replacement of mouse beta(2)m (mbeta(2)m) with hbeta(2)m has several functional consequences for MHC class I complex stability and specificity, but the structural basis for this is presently unknown. To investigate the impact of species-specific beta(2)m subunits on MHC class I conformation, we provide a crystallographic comparison of H-2D(b) in complex with LCMV-derived gp33 peptide and either hbeta(2)m or mbeta(2)m. The conformation of the gp33 peptide is not affected by the beta(2)m species. Comparison of the interface between beta(2)m and the alpha(1)alpha(2) domains of the heavy chain in these two crystal structures reveals a marked increase in both polarity and number of hydrogen bonds between hbeta(2)m and the alpha(1)alpha(2) domains of H-2D(b). We propose that the positioning of two hydrogen bond rich regions at the hbeta(2)m/alpha(1)alpha(2) interface plays a central role in the increased overall stability and peptide exchange capacity in the H-2D(b)/hbeta(2)m complex. These two regions act as bridges, holding and stabilizing the underside of the alpha(1) and alpha(2) helices, enabling a prolonged peptide-receptive conformation of the peptide binding cleft. Furthermore, analysis of H-2D(b) in complex with either mbeta(2)m or hbeta(2)m provides a structural explanation for the differential binding of H-2D(b)/hbeta(2)m to both Ly49A and Ly49C. Our comparative structural study emphasizes the importance of beta(2)m residues at positions 3, 6 and 29 for binding to Ly49A and suggests that sterical hindrance by residue K6 on hbeta(2)m impairs the recognition of Ly49C by H-2D(b)/gp33/hbeta(2)m. Finally, comparison of the two H-2D(b) crystal structures implies that the beta(2)m species may affect the strength of TCR recognition by affecting CD8 binding.
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{{ABSTRACT_PUBMED_16375919}}
==Disease==
==Disease==
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==Reference==
==Reference==
Structural basis of the differential stability and receptor specificity of H-2Db in complex with murine versus human beta2-microglobulin., Achour A, Michaelsson J, Harris RA, Ljunggren HG, Karre K, Schneider G, Sandalova T, J Mol Biol. 2006 Feb 17;356(2):382-96. Epub 2005 Dec 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16375919 16375919]
Structural basis of the differential stability and receptor specificity of H-2Db in complex with murine versus human beta2-microglobulin., Achour A, Michaelsson J, Harris RA, Ljunggren HG, Karre K, Schneider G, Sandalova T, J Mol Biol. 2006 Feb 17;356(2):382-96. Epub 2005 Dec 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16375919 16375919]
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A structural basis for LCMV immune evasion: subversion of H-2D(b) and H-2K(b) presentation of gp33 revealed by comparative crystal structure.Analyses., Achour A, Michaelsson J, Harris RA, Odeberg J, Grufman P, Sandberg JK, Levitsky V, Karre K, Sandalova T, Schneider G, Immunity. 2002 Dec;17(6):757-68. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12479822 12479822]
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Determination of structural principles underlying three different modes of lymphocytic choriomeningitis virus escape from CTL recognition., Velloso LM, Michaelsson J, Ljunggren HG, Schneider G, Achour A, J Immunol. 2004 May 1;172(9):5504-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15100292 15100292]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Murine mhc]]
[[Category: Murine mhc]]
[[Category: Receptor binding]]
[[Category: Receptor binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:32:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:25:24 2008''

Revision as of 12:25, 29 July 2008

Image:2f74.png

Template:STRUCTURE 2f74

Contents

Murine MHC class I H-2Db in complex with human b2-microglobulin and LCMV-derived immunodminant peptide gp33

Template:ABSTRACT PUBMED 16375919

Disease

Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]

About this Structure

2F74 is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

Reference

Structural basis of the differential stability and receptor specificity of H-2Db in complex with murine versus human beta2-microglobulin., Achour A, Michaelsson J, Harris RA, Ljunggren HG, Karre K, Schneider G, Sandalova T, J Mol Biol. 2006 Feb 17;356(2):382-96. Epub 2005 Dec 7. PMID:16375919

A structural basis for LCMV immune evasion: subversion of H-2D(b) and H-2K(b) presentation of gp33 revealed by comparative crystal structure.Analyses., Achour A, Michaelsson J, Harris RA, Odeberg J, Grufman P, Sandberg JK, Levitsky V, Karre K, Sandalova T, Schneider G, Immunity. 2002 Dec;17(6):757-68. PMID:12479822

Determination of structural principles underlying three different modes of lymphocytic choriomeningitis virus escape from CTL recognition., Velloso LM, Michaelsson J, Ljunggren HG, Schneider G, Achour A, J Immunol. 2004 May 1;172(9):5504-11. PMID:15100292

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