1zt7

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{{STRUCTURE_1zt7| PDB=1zt7 | SCENE= }}
{{STRUCTURE_1zt7| PDB=1zt7 | SCENE= }}
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'''crystal structure of class I MHC H-2Kk in complex with a nonapeptide'''
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===crystal structure of class I MHC H-2Kk in complex with a nonapeptide===
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==Overview==
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A wealth of data has accumulated on the structure of mouse MHC class I (MHCI) molecules encoded by the H-2(b) and H-2(d) haplotypes. In contrast, there is a dearth of structural data regarding H-2(k)-encoded molecules. Therefore, the structures of H-2K(k) complexed to an octameric peptide from influenza A virus (HA(259-266)) and to a nonameric peptide from SV40 (SV40(560-568)) have been determined by x-ray crystallography at 2.5 and 3.0 A resolutions, respectively. The structure of the H-2K(k)-HA(259-266) complex reveals that residues located on the floor of the peptide-binding groove contact directly the backbone of the octameric peptide and force it to lie deep within the H-2K(k) groove. This unprecedented mode of peptide binding occurs despite the presence of bulky residues in the middle of the floor of the H-2K(k) peptide-binding groove. As a result, the Calpha atoms of peptide residues P5 and P6 are more buried than the corresponding residues of H-2K(b)-bound octapeptides, making them even less accessible to TCR contact. When bound to H-2K(k), the backbone of the SV40(560-568) nonapeptide bulges out of the peptide-binding groove and adopts a conformation reminiscent of that observed for peptides bound to H-2L(d). This structural convergence occurs despite the totally different architectures of the H-2L(d) and H-2K(k) peptide-binding grooves. Therefore, these two H-2K(k)-peptide complexes provide insights into the mechanisms through which MHC polymorphism outside primary peptide pockets influences the conformation of the bound peptides and have implications for TCR recognition and vaccine design.
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The line below this paragraph, {{ABSTRACT_PUBMED_16148128}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16148128 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16148128}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
The H-2Kk MHC peptide-binding groove anchors the backbone of an octameric antigenic peptide in an unprecedented mode., Kellenberger C, Roussel A, Malissen B, J Immunol. 2005 Sep 15;175(6):3819-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16148128 16148128]
The H-2Kk MHC peptide-binding groove anchors the backbone of an octameric antigenic peptide in an unprecedented mode., Kellenberger C, Roussel A, Malissen B, J Immunol. 2005 Sep 15;175(6):3819-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16148128 16148128]
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Expression, refolding, crystallization and preliminary crystallographic study of MHC H-2Kk complexed with octapeptides and nonapeptides., Kellenberger C, Porciero S, Roussel A, Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1278-80. Epub 2004, Jun 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15213391 15213391]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Roussel, A.]]
[[Category: Roussel, A.]]
[[Category: Peptide binding groove]]
[[Category: Peptide binding groove]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:02:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:26:21 2008''

Revision as of 18:26, 27 July 2008

Image:1zt7.png

Template:STRUCTURE 1zt7

crystal structure of class I MHC H-2Kk in complex with a nonapeptide

Template:ABSTRACT PUBMED 16148128

About this Structure

1ZT7 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

The H-2Kk MHC peptide-binding groove anchors the backbone of an octameric antigenic peptide in an unprecedented mode., Kellenberger C, Roussel A, Malissen B, J Immunol. 2005 Sep 15;175(6):3819-25. PMID:16148128

Expression, refolding, crystallization and preliminary crystallographic study of MHC H-2Kk complexed with octapeptides and nonapeptides., Kellenberger C, Porciero S, Roussel A, Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1278-80. Epub 2004, Jun 22. PMID:15213391

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