S
S. W. Cowan
Researcher at Uppsala University
Publications - 5
Citations - 1373
S. W. Cowan is an academic researcher from Uppsala University. The author has contributed to research in topics: Protein structure & Binding site. The author has an hindex of 5, co-authored 5 publications receiving 1349 citations.
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Book ChapterDOI
Lipid-Binding Proteins: A Family of Fatty Acid and Retinoid Transport Proteins
Leonard J. Banaszak,Nathan S. Winter,Zhaohui Xu,David A. Bernlohr,S. W. Cowan,Alwyn T. Jones +5 more
TL;DR: This chapter focuses on the structural analyses and comparisons between members of a multigene family of hydrophobic ligand-binding proteins and provides a detailed comparison of intra- and extracellular lipid binding proteins with known crystal structures.
Journal ArticleDOI
Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes.
Irmgard Sinning,Gerard J. Kleywegt,S. W. Cowan,Peter Reinemer,H.W. Dirr,Robert Huber,Gary L. Gilliland,Richard N. Armstrong,Xinhua Ji,Philip G. Board,B. Olin,Bengt Mannervik,T.A. Jones +12 more
TL;DR: The structure shows an overall similarity to the mu and pi class enzymes particularly in the glutathione-binding domain, but the main difference concerns the extended C terminus of the alpha class enzyme which forms an extra alpha-helix that blocks one entrance to the active site and makes up part of the substrate binding site.
Journal ArticleDOI
Crystallographic refinement of human serum retinol binding protein at 2A resolution.
TL;DR: The structural basis for the conservation of sequence within the family of proteins is described, many of which are carrier proteins for smaller ligand molecules.
Journal ArticleDOI
Crystallographic Studies on a Family of Cellular Lipophilic Transport Proteins: Refinement of P2 Myelin Protein and the Structure Determination and Refinement of Cellular Retinol-binding Protein in Complex with All-trans-retinol
TL;DR: P2 myelin protein (P2) and cellular retinol binding protein (CRBP) are members of a family of cellular lipophilic transport proteins that form a compact three-dimensional structure built up from ten antiparallel strands that fold to form an orthogonal barrel containing the ligand.
Journal ArticleDOI
Crystallization of GST2, a human class alpha glutathione transferase
S. W. Cowan,Terese Bergfors,T. Alwyn Jones,Gudrun Tibbelin,B. Olin,Philip G. Board,Bengt Mannervik +6 more
TL;DR: Single crystals of human GST2, a class alpha glutathione transferase have been grown in polyethylene glycol 2000 by the hanging-drop vapour diffusion method and the X-ray diffraction pattern extends to better than 3 A resolution.