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- Noresson, A. L., et al.
(författare)
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Designing interactions by control of protein-ligand complex conformation : Tuning arginine-arene interaction geometry for enhanced electrostatic protein-ligand interactions
- 2018
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Ingår i: Chemical Science. - : Royal Society of Chemistry (RSC). - 2041-6520 .- 2041-6539. ; 9:4, s. 1014-1021
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Tidskriftsartikel (refereegranskat)abstract
- We investigated galectin-3 binding to 3-benzamido-2-O-sulfo-galactoside and -thiodigalactoside ligands using a combination of site-specific mutagenesis, X-ray crystallography, computational approaches, and binding thermodynamics measurements. The results reveal a conformational variability in a surface-exposed arginine (R144) side chain in response to different aromatic C3-substituents of bound galactoside-based ligands. Fluorinated C3-benzamido substituents induced a shift in the side-chain conformation of R144 to allow for an entropically favored electrostatic interaction between its guanidine group and the 2-O-sulfate of the ligand. By contrast, binding of ligands with non-fluorinated substituents did not trigger a conformational change of R144. Hence, a sulfate-arginine electrostatic interaction can be tuned by the choice of ligand C3-benzamido structures to favor specific interaction modes and geometries. These results have important general implications for ligand design, as the proper choice of arginine-aromatic interacting partners opens up for ligand-controlled protein conformation that in turn may be systematically exploited in ligand design.
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3. |
- Lundgren, T, et al.
(författare)
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Pet in clinical islet transplantation
- 2009
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Ingår i: XENOTRANSPLANTATION. - 0908-665X. ; 16:5, s. 295-295
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Konferensbidrag (övrigt vetenskapligt/konstnärligt)
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4. |
- Langstrom, B, et al.
(författare)
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PET i klinisk verksamhet.
- 1995
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Ingår i: Läkartidningen. ; 92, s. 3202-
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)
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