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Atomic mapping of t...
Atomic mapping of the sugar interactions in one-site and two-site mutants of Cyanovirin-N by NMR spectroscopy
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- Sandstrom, Corine (författare)
- Swedish Univ Agr Sci, Dept Chem, SE-75007 Uppsala, Sweden.
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- Hakkarainen, Birgit (författare)
- Swedish Univ Agr Sci, Dept Chem, SE-75007 Uppsala, Sweden.
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- Matei, Elena (författare)
- Univ Pittsburgh, Sch Med, Dept Biol Struct, Pittsburgh, PA 15261 USA.
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- Glinchert, Anja (författare)
- Univ Coll Dublin, Ctr Synthesis & Chem Biol, Dublin 4, Ireland.
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- Lahmann, Martina (författare)
- Univ Bangor, Sch Chem, Bangor LL57 2UW, Gwynedd, Wales.
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- Oscarson, Stefan (författare)
- Univ Coll Dublin, Ctr Synthesis & Chem Biol, Dublin 4, Ireland.
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- Kenne, Lennart (författare)
- Swedish Univ Agr Sci, Dept Chem, SE-75007 Uppsala, Sweden.
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- Gronenborn, Angela M. (författare)
- Univ Pittsburgh, Sch Med, Dept Biol Struct, Pittsburgh, PA 15261 USA.
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Swedish Univ Agr Sci, Dept Chem, SE-75007 Uppsala, Sweden Univ Pittsburgh, Sch Med, Dept Biol Struct, Pittsburgh, PA 15261 USA. (creator_code:org_t)
- 2008-03-01
- 2008
- Engelska.
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Ingår i: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 47:12, s. 3625-3635
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- The details of the interaction between two mutants of Cyanovirin-N (CV-N), an HIV inactivating protein, and di- and trimannosides, substructures of Man-9, were investigated by STD NMR. spectroscopy. One mutant, CV-N-mutDB, contains only one carbohydrate-binding site on domain A, whereas in CV-N-mutDA, the specificity of domain A for trimannose was changed while the site in domain B was kept intact, allowing for a dissection of the overall binding. Results of the STD NMR experiments revealed close contact between the protein binding site on domain A and H2, H3, and H4 of the nonreducing terminal mannose unit for Man alpha(1-2)Man alpha OMe, Man alpha(1-2)Man alpha(1-3)Man alpha OMe, and Man alpha(1-2)Man alpha(1-6)Man alpha OMe. The Man alpha(1-2)Man alpha(1-2)Man alpha OMe trisaccharide interacted with CV-N with the highest affinity. Further dissection of the interaction was achieved by NMR experiments with synthetic 2'-, 3'-, 4'-, and 6'-deoxy analogues of the disaccharide Man alpha(1-2)Man alpha OMe. STD and H-1-N-15 HSQC NMR spectroscopy revealed that the 2'- and 6'-deoxy dimannosides were recognized by CV-N, whereas no binding was detected for the 3'- and 4'-deoxy sugars. These results demonstrate that the 3'- and 4'-hydroxyl groups on the terminal residue are engaged in key polar interactions with the protein and are required for high-affinity binding.
Ämnesord
- NATURVETENSKAP -- Kemi -- Organisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Organic Chemistry (hsv//eng)
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