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Crystal structure o...
Crystal structure of a SEA variant in complex with MHC class II reveals the ability of SEA to crosslink MHC molecules
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- Lindkvist, Karin (författare)
- Lund University,Lunds universitet,Medicinsk strukturbiologi,Forskargrupper vid Lunds universitet,Medical Structural Biology,Lund University Research Groups
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- Thunnissen, Marjolein (författare)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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Forsberg, G (författare)
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Walse, B (författare)
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(creator_code:org_t)
- 2002
- 2002
- Engelska.
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Ingår i: Structure. - 0969-2126. ; 10:12, s. 1619-1626
- Relaterad länk:
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http://dx.doi.org/10...
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https://lup.lub.lu.s...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Although the biological properties of staphylococcal enterotoxin A (SEA) have been well characterized, structural insights into the interaction between SEA and major histocompatibilty complex (MHC) class II have only been obtained by modeling. Here, the crystal structure of the D227A variant of SEA in complex with human MHC class II has been determined by X-ray crystallography. SEA(D227A) exclusively binds with its N-terminal domain to the alpha chain of HLA-DR1. The ability of one SEA molecule to crosslink two MHC molecules was modeled. It shows that this SEA molecule cannot interact with the T cell receptor (TCR) while a second SEA molecule interacts with MHC. Because of its relatively low toxicity, the D227A variant of SEA is used in tumor therapy.
Ämnesord
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Nyckelord
- enterotoxin
- staphylococcal
- SEA
- MHC class II
- protein-protein interaction
- superantigen
- X-ray crystallography
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
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