This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1a1n

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1a1n.gif|left|200px]]<br />
+
[[Image:1a1n.gif|left|200px]]<br /><applet load="1a1n" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="1a1n" size="450" color="white" frame="true" align="right" spinBox="true"
+
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==
-
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.
+
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==
Line 11: Line 10:
==About this Structure==
==About this Structure==
-
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].
+
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==
Line 18: Line 17:
[[Category: Human immunodeficiency virus 1]]
[[Category: Human immunodeficiency virus 1]]
[[Category: Protein complex]]
[[Category: Protein complex]]
-
[[Category: Bell, J.I.]]
+
[[Category: Bell, J I.]]
-
[[Category: Jones, E.Y.]]
+
[[Category: Jones, E Y.]]
-
[[Category: Mcmichael, A.J.]]
+
[[Category: Mcmichael, A J.]]
-
[[Category: Reid, S.W.]]
+
[[Category: Reid, S W.]]
-
[[Category: Smith, K.J.]]
+
[[Category: Smith, K J.]]
-
[[Category: Stuart, D.I.]]
+
[[Category: Stuart, D I.]]
[[Category: complex (antigen/peptide)]]
[[Category: complex (antigen/peptide)]]
[[Category: hiv]]
[[Category: hiv]]
Line 32: Line 31:
[[Category: nef]]
[[Category: nef]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 15:54:20 2007''
+
''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

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Thu Feb 21 11:39:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools