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1xh3

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==Overview==
==Overview==
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Human HLA-B*3501 binds an antigenic peptide of 14-aa length derived from, an alternative reading frame of M-CSF with high affinity. Due to its, extraordinary length, the exact HLA binding mode was unpredictable. The, crystal structure of HLA-B*3501 at 1.5 A shows that the N and C termini of, the peptide are embedded in the A and F pockets, respectively, similar to, a peptide of normal length. The central part of the 14-meric peptide, bulges flexibly out of the groove. Two variants of the alternative reading, frame of M-CSF peptide substituted at P2 or P2 and P9 with Ala display, weak or no T cell activation. Their structure differs mainly in, flexibility and conformation from the agonistic peptide. Moreover, the, variants induce subtle changes of MHC alpha-helical regions implicated as, critical for TCR contact. The TCR specifically recognizing this, peptide/MHC complex exhibits CDR3 length within the normal range, suggesting major conformational adaptations of this receptor upon, peptide/MHC binding. Thus, the potential antigenic repertoire recognizable, by CTLs is larger than currently thought.
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Human HLA-B*3501 binds an antigenic peptide of 14-aa length derived from an alternative reading frame of M-CSF with high affinity. Due to its extraordinary length, the exact HLA binding mode was unpredictable. The crystal structure of HLA-B*3501 at 1.5 A shows that the N and C termini of the peptide are embedded in the A and F pockets, respectively, similar to a peptide of normal length. The central part of the 14-meric peptide bulges flexibly out of the groove. Two variants of the alternative reading frame of M-CSF peptide substituted at P2 or P2 and P9 with Ala display weak or no T cell activation. Their structure differs mainly in flexibility and conformation from the agonistic peptide. Moreover, the variants induce subtle changes of MHC alpha-helical regions implicated as critical for TCR contact. The TCR specifically recognizing this peptide/MHC complex exhibits CDR3 length within the normal range, suggesting major conformational adaptations of this receptor upon peptide/MHC binding. Thus, the potential antigenic repertoire recognizable by CTLs is larger than currently thought.
==Disease==
==Disease==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Eynde, B.J.van.den.]]
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[[Category: Eynde, B J.van den.]]
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[[Category: Hecht, H.J.]]
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[[Category: Hecht, H J.]]
[[Category: Herrmann, H.]]
[[Category: Herrmann, H.]]
[[Category: Janke, V.]]
[[Category: Janke, V.]]
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[[Category: immune system]]
[[Category: immune system]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:09:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:54:42 2008''

Revision as of 13:54, 21 February 2008


1xh3, resolution 1.48Å

Drag the structure with the mouse to rotate

Conformational Restraints and Flexibility of 14-Meric Peptides in Complex with HLA-B*3501

Contents

Overview

Human HLA-B*3501 binds an antigenic peptide of 14-aa length derived from an alternative reading frame of M-CSF with high affinity. Due to its extraordinary length, the exact HLA binding mode was unpredictable. The crystal structure of HLA-B*3501 at 1.5 A shows that the N and C termini of the peptide are embedded in the A and F pockets, respectively, similar to a peptide of normal length. The central part of the 14-meric peptide bulges flexibly out of the groove. Two variants of the alternative reading frame of M-CSF peptide substituted at P2 or P2 and P9 with Ala display weak or no T cell activation. Their structure differs mainly in flexibility and conformation from the agonistic peptide. Moreover, the variants induce subtle changes of MHC alpha-helical regions implicated as critical for TCR contact. The TCR specifically recognizing this peptide/MHC complex exhibits CDR3 length within the normal range, suggesting major conformational adaptations of this receptor upon peptide/MHC binding. Thus, the potential antigenic repertoire recognizable by CTLs is larger than currently thought.

Disease

Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142830], Hypoproteinemia, hypercatabolic OMIM:[109700], Spondyloarthropathy, susceptibility to, 1 OMIM:[142830], Stevens-Johnson syndrome, carbamazepine-induced, susceptibility to OMIM:[142830]

About this Structure

1XH3 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Conformational restraints and flexibility of 14-meric peptides in complex with HLA-B*3501., Probst-Kepper M, Hecht HJ, Herrmann H, Janke V, Ocklenburg F, Klempnauer J, van den Eynde BJ, Weiss S, J Immunol. 2004 Nov 1;173(9):5610-6. PMID:15494511

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