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Novel binding site ...
Novel binding site identified in a hybrid between cholera toxin and heat-labile enterotoxin: 1.9 A crystal structure reveals the details.
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- Holmner, Åsa (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Lebens, Michael, 1956 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för medicinsk mikrobiologi och immunologi,Institute of Medical Microbiology/Immunology,University of Gothenburg
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- Teneberg, Susann, 1955 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för medicinsk och fysiologisk kemi,Institute of Medical Biochemistry,University of Gothenburg
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- Ångström, Jonas, 1950 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för medicinsk och fysiologisk kemi,Institute of Medical Biochemistry,University of Gothenburg
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- Ökvist, Mats, 1970 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry,University of Gothenburg
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- Krengel, Ute, 1964 (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
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(creator_code:org_t)
- Elsevier BV, 2004
- 2004
- Engelska.
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Ingår i: Structure (London, England : 1993). - : Elsevier BV. - 0969-2126 .- 1878-4186. ; 12:9, s. 1655-67
- Relaterad länk:
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http://www.cell.com/...
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http://dx.doi.org/10...
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https://gup.ub.gu.se...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- A hybrid between the B subunits of cholera toxin and Escherichia coli heat-labile enterotoxin has been described, which exhibits a novel binding specificity to blood group A and B type 2 determinants. In the present investigation, we have determined the crystal structure of this protein hybrid, termed LCTBK, in complex with the blood group A pentasaccharide GalNAcalpha3(Fucalpha2)Galbeta4(Fucalpha3)GlcNAcbeta, confirming not only the novel binding specificity but also a distinct new oligosaccharide binding site. Binding studies revealed that the new specificity can be ascribed to a single mutation (S4N) introduced into the sequence of Escherichia coli heat-labile enterotoxin. At a resolution of 1.9 A, the new binding site is resolved in excellent detail. Main features include a complex network of water molecules, which is well preserved by the parent toxins, and an unexpectedly modest contribution to binding by the critical residue Asn4, which interacts with the ligand only via a single water molecule.
Nyckelord
- Asparagine
- metabolism
- Bacterial Toxins
- chemistry
- genetics
- metabolism
- Binding Sites
- Blood Group Antigens
- metabolism
- Cholera Toxin
- chemistry
- genetics
- metabolism
- Crystallography
- X-Ray
- Drug Design
- Enterotoxins
- chemistry
- genetics
- metabolism
- Escherichia coli Proteins
- chemistry
- genetics
- metabolism
- Glycosphingolipids
- chemistry
- metabolism
- Humans
- Models
- Molecular
- Molecular Sequence Data
- Molecular Structure
- Oligosaccharides
- chemistry
- metabolism
- Protein Binding
- Protein Structure
- Tertiary
- Protein Subunits
- chemistry
- genetics
- metabolism
- Recombinant Fusion Proteins
- chemistry
- genetics
- metabolism
- Water
- chemistry
- Water
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas
- Av författaren/redakt...
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Holmner, Åsa
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Lebens, Michael, ...
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Teneberg, Susann ...
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Ångström, Jonas, ...
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Ökvist, Mats, 19 ...
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Krengel, Ute, 19 ...
- Artiklar i publikationen
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Structure (Londo ...
- Av lärosätet
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Göteborgs universitet
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Chalmers tekniska högskola