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The folding and stability of human alpha class glutathione transferase A1-1 depend on distinct roles of a conserved N-capping box and hydrophobic staple motif
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Biochemistry.
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2001 (English)In: JOURNAL OF BIOLOGICAL CHEMISTRY, ISSN 0021-9258, Vol. 276, no 34, 32177-32183 p.Article in journal (Refereed) Published
Abstract [en]

An N-capping box and a hydrophobic staple motif are strictly conserved in the core of all known glutathione S-transferases (GST). In the present work, mutations of hGSTA1-1 enzyme residues forming these motifs have been generated. The analysis of S154A, D

Place, publisher, year, edition, pages
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC , 2001. Vol. 276, no 34, 32177-32183 p.
Keyword [en]
S-TRANSFERASE; TRANSITION-STATE; CHYMOTRYPSIN INHIBITOR-2; 3-DIMENSIONAL STRUCTURE; IDENTIFICATION; ISOENZYMES; RESIDUES; NUCLEUS; P1-1; MECHANISMS
Identifiers
URN: urn:nbn:se:uu:diva-38010OAI: oai:DiVA.org:uu-38010DiVA: diva2:65909
Note
Addresses: Aceto A, Univ G DAnnunzio, Dipartimento Sci Biochim, Via Vestini 31, I-66100 Chieti, Italy. Univ G DAnnunzio, Dipartimento Sci Biochim, I-66100 Chieti, Italy. Univ G DAnnunzio, Dipartimento Sci Farmaco, I-66100 Chieti, Italy. Uppsala Univ, DeptAvailable from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14

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