1jpf
From Proteopedia
(New page: 200px<br /><applet load="1jpf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jpf, resolution 2.18Å" /> '''Crystal Structure Of...) |
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| - | [[Image:1jpf.jpg|left|200px]]<br /><applet load="1jpf" size=" | + | [[Image:1jpf.jpg|left|200px]]<br /><applet load="1jpf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jpf, resolution 2.18Å" /> | caption="1jpf, resolution 2.18Å" /> | ||
'''Crystal Structure Of The LCMV Peptidic Epitope Gp276 In Complex With The Murine Class I Mhc Molecule H-2Db'''<br /> | '''Crystal Structure Of The LCMV Peptidic Epitope Gp276 In Complex With The Murine Class I Mhc Molecule H-2Db'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Class I major histocompatibility complex (MHC) molecules, which display | + | Class I major histocompatibility complex (MHC) molecules, which display intracellularly processed peptides on the cell surface for scanning by T-cell receptors (TCRs), are extraordinarily polymorphic. MHC polymorphism is believed to result from natural selection, since individuals heterozygous at the corresponding loci can cope with a larger number of pathogens. Here, we present the crystal structures of the murine MHC molecule H-2D(b) in complex with the peptides gp276 and np396 from the lymphocytic choriomeningitis virus (LCMV), solved at 2.18 A and 2.20 A resolution, respectively. The most prominent feature of H-2D(b) is a hydrophobic ridge that cuts across its antigen-binding site, which is conserved in the L(d)-like family of class I MHC molecules. The comparison with previously solved crystal structures of peptide/H-2D(b) complexes shows that the hydrophobic ridge focuses the conformational variability of the bound peptides in a "hot-spot", which could allow optimal TCR interaction and discrimination. This finding suggests a functional reason for the conservation of this structural element. |
==About this Structure== | ==About this Structure== | ||
| - | 1JPF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1JPF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JPF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Capitani, G.]] | [[Category: Capitani, G.]] | ||
[[Category: Ciatto, C.]] | [[Category: Ciatto, C.]] | ||
| - | [[Category: Grutter, M | + | [[Category: Grutter, M G.]] |
[[Category: Pecorari, F.]] | [[Category: Pecorari, F.]] | ||
[[Category: Pluckthun, A.]] | [[Category: Pluckthun, A.]] | ||
| - | [[Category: Tissot, A | + | [[Category: Tissot, A C.]] |
[[Category: Tschopp, M.]] | [[Category: Tschopp, M.]] | ||
[[Category: ig fold]] | [[Category: ig fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:12 2008'' |
Revision as of 11:25, 21 February 2008
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Crystal Structure Of The LCMV Peptidic Epitope Gp276 In Complex With The Murine Class I Mhc Molecule H-2Db
Overview
Class I major histocompatibility complex (MHC) molecules, which display intracellularly processed peptides on the cell surface for scanning by T-cell receptors (TCRs), are extraordinarily polymorphic. MHC polymorphism is believed to result from natural selection, since individuals heterozygous at the corresponding loci can cope with a larger number of pathogens. Here, we present the crystal structures of the murine MHC molecule H-2D(b) in complex with the peptides gp276 and np396 from the lymphocytic choriomeningitis virus (LCMV), solved at 2.18 A and 2.20 A resolution, respectively. The most prominent feature of H-2D(b) is a hydrophobic ridge that cuts across its antigen-binding site, which is conserved in the L(d)-like family of class I MHC molecules. The comparison with previously solved crystal structures of peptide/H-2D(b) complexes shows that the hydrophobic ridge focuses the conformational variability of the bound peptides in a "hot-spot", which could allow optimal TCR interaction and discrimination. This finding suggests a functional reason for the conservation of this structural element.
About this Structure
1JPF is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Zooming in on the hydrophobic ridge of H-2D(b): implications for the conformational variability of bound peptides., Ciatto C, Tissot AC, Tschopp M, Capitani G, Pecorari F, Pluckthun A, Grutter MG, J Mol Biol. 2001 Oct 5;312(5):1059-71. PMID:11580250
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