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| - | [[Image:2fwo.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2fwo.png|left|200px]] |
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| | {{STRUCTURE_2fwo| PDB=2fwo | SCENE= }} | | {{STRUCTURE_2fwo| PDB=2fwo | SCENE= }} |
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| - | '''MHC Class I H-2Kd heavy chain in complex with beta-2microglobulin and peptide derived from influenza nucleoprotein'''
| + | ===MHC Class I H-2Kd heavy chain in complex with beta-2microglobulin and peptide derived from influenza nucleoprotein=== |
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| - | ==Overview==
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| - | Classic major histocompatibility complex (MHC) proteins associate with antigen- and self-derived peptides in an allele-specific manner. Herein we present the crystal structure of the MHC class I protein H-2K(d) (K(d)) expressed by BALB/c mice in complex with an antigenic peptide derived from influenza A/PR/8/34 nucleoprotein (Flu, residues 147-155, TYQRTRALV). Analysis of our structure in conjunction with the sequences of naturally processed epitopes provides a comprehensive understanding of the dominant K(d) peptide-binding motif. We find that Flu residues Tyr(P2), Thr(P5), and Val(P9) are sequestered into the B, C, and F pockets of the K(d) groove, respectively. The shape and chemistry of the polymorphic B pocket make it an optimal binding site for the side chain of Tyr(P2) as the dominant anchoring residue of nonameric peptides. The non-polar F pocket limits the amino acid repertoire at P9 to hydrophobic residues such as Ile, Leu, or Val, whereas the C pocket restricts the size of the P5-anchoring side chain. We also show that Flu is accommodated in the complex through an unfavorable kink in the otherwise extended peptide backbone due to the presence of a prominent ridge in the K(d) groove. Surprisingly, this backbone conformation is strikingly similar to D(b)-presented peptides despite the fact that these proteins employ distinct motif-anchoring strategies. The results presented in this study provide a solid foundation for the understanding of K(d)-restricted antigen presentation and recognition events.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16473882}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16473882 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16473882}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Antigens/peptides/epitope]] | | [[Category: Antigens/peptides/epitope]] |
| | [[Category: Mhc]] | | [[Category: Mhc]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:23:31 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:30:47 2008'' |
Revision as of 07:30, 28 July 2008
Template:STRUCTURE 2fwo
MHC Class I H-2Kd heavy chain in complex with beta-2microglobulin and peptide derived from influenza nucleoprotein
Template:ABSTRACT PUBMED 16473882
About this Structure
2FWO is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural definition of the H-2Kd peptide-binding motif., Mitaksov V, Fremont DH, J Biol Chem. 2006 Apr 14;281(15):10618-25. Epub 2006 Feb 10. PMID:16473882
Page seeded by OCA on Mon Jul 28 10:30:47 2008
