1a1n

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[[Image:1a1n.gif|left|200px]]<br />
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[[Image:1a1n.gif|left|200px]]<br /><applet load="1a1n" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1a1n" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1a1n, resolution 2.0&Aring;" />
caption="1a1n, resolution 2.0&Aring;" />
'''MHC CLASS I MOLECULE B*3501 COMPLEXED WITH PEPTIDE VPLRPMTY FROM THE NEF PROTEIN (75-82) OF HIV1'''<br />
'''MHC CLASS I MOLECULE B*3501 COMPLEXED WITH PEPTIDE VPLRPMTY FROM THE NEF PROTEIN (75-82) OF HIV1'''<br />
==Overview==
==Overview==
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The crystal structure of the human major histocompatibility complex class, I B allele HLA B*3501 complexed with the 8-mer peptide epitope HIV1 Nef, 75-82 (VPLRPMTY) has been determined at 2.0 angstrom resolution., Comparison with the crystal structure of the closely related allele HLA, B*5301 reveals the structural basis for the tyrosine specificity of the, B*3501 F pocket. The structure also reveals a novel conformation of the, 8-mer peptide within the binding groove. The positions of the peptide N, and C termini are nonstandard, but the classic pattern of hydrogen bonding, to nonpolymorphic MHC class I residues is maintained, at the N terminus by, addition of a water molecule, and at the C terminus by a substantial shift, in the alpha 2 helix.
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The crystal structure of the human major histocompatibility complex class I B allele HLA B*3501 complexed with the 8-mer peptide epitope HIV1 Nef 75-82 (VPLRPMTY) has been determined at 2.0 angstrom resolution. Comparison with the crystal structure of the closely related allele HLA B*5301 reveals the structural basis for the tyrosine specificity of the B*3501 F pocket. The structure also reveals a novel conformation of the 8-mer peptide within the binding groove. The positions of the peptide N and C termini are nonstandard, but the classic pattern of hydrogen bonding to nonpolymorphic MHC class I residues is maintained, at the N terminus by addition of a water molecule, and at the C terminus by a substantial shift in the alpha 2 helix.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1A1N is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A1N OCA].
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1A1N is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A1N OCA].
==Reference==
==Reference==
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[[Category: Human immunodeficiency virus 1]]
[[Category: Human immunodeficiency virus 1]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Bell, J.I.]]
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[[Category: Bell, J I.]]
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[[Category: Jones, E.Y.]]
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[[Category: Jones, E Y.]]
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[[Category: Mcmichael, A.J.]]
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[[Category: Mcmichael, A J.]]
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[[Category: Reid, S.W.]]
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[[Category: Reid, S W.]]
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[[Category: Smith, K.J.]]
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[[Category: Smith, K J.]]
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[[Category: Stuart, D.I.]]
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[[Category: Stuart, D I.]]
[[Category: complex (antigen/peptide)]]
[[Category: complex (antigen/peptide)]]
[[Category: hiv]]
[[Category: hiv]]
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[[Category: nef]]
[[Category: nef]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 15:54:20 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:49 2008''

Revision as of 09:39, 21 February 2008


1a1n, resolution 2.0Å

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MHC CLASS I MOLECULE B*3501 COMPLEXED WITH PEPTIDE VPLRPMTY FROM THE NEF PROTEIN (75-82) OF HIV1

Contents

Overview

The crystal structure of the human major histocompatibility complex class I B allele HLA B*3501 complexed with the 8-mer peptide epitope HIV1 Nef 75-82 (VPLRPMTY) has been determined at 2.0 angstrom resolution. Comparison with the crystal structure of the closely related allele HLA B*5301 reveals the structural basis for the tyrosine specificity of the B*3501 F pocket. The structure also reveals a novel conformation of the 8-mer peptide within the binding groove. The positions of the peptide N and C termini are nonstandard, but the classic pattern of hydrogen bonding to nonpolymorphic MHC class I residues is maintained, at the N terminus by addition of a water molecule, and at the C terminus by a substantial shift in the alpha 2 helix.

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

1A1N is a Protein complex structure of sequences from Homo sapiens and Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

Reference

An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501., Smith KJ, Reid SW, Stuart DI, McMichael AJ, Jones EY, Bell JI, Immunity. 1996 Mar;4(3):203-13. PMID:8624811

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