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Structural basis fo...
Structural basis for detoxification and oxidative stress protection in membranes
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- Holm, Peter (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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Bhakat, Priyaranjan (författare)
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- Jegerschold, Caroline (författare)
- Karolinska Institutet
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Gyobu, Nobuhiko (författare)
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Mitsuoka, Kaoru (författare)
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Fujiyoshi, Yoshinori (författare)
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- Morgenstern, Ralf (författare)
- Karolinska Institutet
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- Hebert, Hans (författare)
- Karolinska Institutet,Lund University,Lunds universitet,KTH,Strukturell bioteknik,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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(creator_code:org_t)
- Elsevier BV, 2006
- 2006
- Engelska.
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Ingår i: Journal of Molecular Biology. - : Elsevier BV. - 0022-2836 .- 1089-8638. ; 360:5, s. 934-945
- Relaterad länk:
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http://dx.doi.org/10...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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https://lup.lub.lu.s...
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http://kipublication...
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Abstract
Ämnesord
Stäng
- Synthesis of mediators of fever, pain and inflammation as well as protection against reactive molecules and oxidative stress is a hallmark of the MAPEG superfamily (membrane associated proteins in eicosanoid and glutathione metabolism). The structure of a MAPEG member, rat mictosomal glutathione transferase 1, at 3.2 angstrom resolution, solved here in complex with glutathione by electron crystallography, defines the active site location and a cytosolic domain involved in enzyme activation. The glutathione binding site is found to be different from that of the canonical soluble glutathione transferases. The architecture of the homotrimer supports a catalytic mechanism involving subunit interactions and reveals both cytosolic and membraneous substrate entry sites, providing a rationale for the membrane location of the enzyme.
Ämnesord
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Nyckelord
- membrane protein
- oxidative stress
- enzymology
- protein structure
- electron crystallography
- microsomal glutathione transferase
- leukotriene c-4 synthase
- 6 angstrom resolution
- s-transferase
- electron crystallography
- purification
- activation
- substrate
- superfamily
- microscopy
- electron crystallography
- protein structure
- enzymology
- membrane protein
- oxidative stress
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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