1dyq

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==Overview==
==Overview==
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Staphylococcal enterotoxins (SEs) are superantigenic protein toxins, responsible for a number of life-threatening diseases. The X-ray structure, of a staphylococcal enterotoxin A (SEA) triple-mutant (L48R, D70R, and, Y92A) vaccine reveals a cascade of structural rearrangements located in, three loop regions essential for binding the alpha subunit of major, histocompatibility complex class II (MHC-II) molecules. A comparison of, hypothetical model complexes between SEA and the SEA triple mutant with, MHC-II HLA-DR1 clearly shows disruption of key ionic and hydrophobic, interactions necessary for forming the complex. Extensive dislocation of, the disulfide loop in particular interferes with MHC-IIalpha binding. The, triple-mutant structure provides new insights into the loss of, superantigenicity and toxicity of an engineered superantigen and provides, a basis for further design of enterotoxin vaccines.
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Staphylococcal enterotoxins (SEs) are superantigenic protein toxins responsible for a number of life-threatening diseases. The X-ray structure of a staphylococcal enterotoxin A (SEA) triple-mutant (L48R, D70R, and Y92A) vaccine reveals a cascade of structural rearrangements located in three loop regions essential for binding the alpha subunit of major histocompatibility complex class II (MHC-II) molecules. A comparison of hypothetical model complexes between SEA and the SEA triple mutant with MHC-II HLA-DR1 clearly shows disruption of key ionic and hydrophobic interactions necessary for forming the complex. Extensive dislocation of the disulfide loop in particular interferes with MHC-IIalpha binding. The triple-mutant structure provides new insights into the loss of superantigenicity and toxicity of an engineered superantigen and provides a basis for further design of enterotoxin vaccines.
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: Krupka, H.I.]]
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[[Category: Krupka, H I.]]
[[Category: Rupp, B.]]
[[Category: Rupp, B.]]
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[[Category: Segelke, B.W.]]
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[[Category: Segelke, B W.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: vaccine]]
[[Category: vaccine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:36:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:21:55 2008''

Revision as of 10:21, 21 February 2008


1dyq, resolution 1.50Å

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STAPHYLOCOCCAL ENTEROTOXIN A MUTANT VACCINE

Overview

Staphylococcal enterotoxins (SEs) are superantigenic protein toxins responsible for a number of life-threatening diseases. The X-ray structure of a staphylococcal enterotoxin A (SEA) triple-mutant (L48R, D70R, and Y92A) vaccine reveals a cascade of structural rearrangements located in three loop regions essential for binding the alpha subunit of major histocompatibility complex class II (MHC-II) molecules. A comparison of hypothetical model complexes between SEA and the SEA triple mutant with MHC-II HLA-DR1 clearly shows disruption of key ionic and hydrophobic interactions necessary for forming the complex. Extensive dislocation of the disulfide loop in particular interferes with MHC-IIalpha binding. The triple-mutant structure provides new insights into the loss of superantigenicity and toxicity of an engineered superantigen and provides a basis for further design of enterotoxin vaccines.

About this Structure

1DYQ is a Single protein structure of sequence from Staphylococcus aureus with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Structural basis for abrogated binding between staphylococcal enterotoxin A superantigen vaccine and MHC-IIalpha., Krupka HI, Segelke BW, Ulrich RG, Ringhofer S, Knapp M, Rupp B, Protein Sci. 2002 Mar;11(3):642-51. PMID:11847286

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