Related ArticlesMolecular analysis of sialoside binding to sialoadhesin by NMR and site-directed mutagenesis.
Biochem J. 1999 Jul 15;341 ( Pt 2):355-61
Authors: Crocker PR, Vinson M, Kelm S, Drickamer K
The molecular interactions between sialoadhesin and sialylated ligands have been investigated by using proton NMR. Addition of ligands to the 12 kDa N-terminal immunoglobulin-like domain of sialoadhesin result in resonance shifts in the protein spectrum that have been used to determine the affinities of sialoadhesin for several sialosides. The results indicate that alpha2, 3-sialyl-lactose and alpha2,6-sialyl-lactose bind respectively 2- and 1.5-fold more strongly than does alpha-methyl-N-acetylneuraminic acid (alpha-Me-NeuAc). The resonances corresponding to the methyl protons within the N-acetyl moiety of sialic acid undergo upfield shifting and broadening during titrations, reflecting an interaction of this group with Trp2 in sialoadhesin as observed in co-crystals of the terminal domain with bound ligand. This resonance shift was used to measure the affinities of mutant and wild-type forms of sialoadhesin in which the first three domains are fused to the Fc region of human IgG1. Substitution of Arg97 by alanine completely abrogated measurable interaction with alpha-Me-NeuAc, whereas a conservative substitution with lysine resulted in a 10-fold decrease in affinity. These results provide the first direct measurement of the affinity of sialoadhesin for sialosides and confirm the critical importance of the conserved arginine in interactions between sialosides and members of the siglec family of sialic acid-binding, immunoglobulin-like lectins.
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supra-Molecular Protein Systems: Applications to the Proteasome and to the ClpP Protease.
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Methyl groups are powerful reporters of structure, motion and function in NMR studies of supra-molecular protein assemblies. Their...
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Proteins. 2005 May 1;59(2):347-55
Authors: le Maire A, Weber T, Saunier S, Broutin I, Antignac C, Ducruix A, Dardel F
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J Biochem. 2000 Apr;127(4):681-6
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Biochemistry. 1996 Jul 30;35(30):9637-46
Authors: Scheuring J, Fischer M, Cushman M, Lee J, Bacher A,...
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[NMR paper] Heparin binding to platelet factor-4. An NMR and site-directed mutagenesis study: arg
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Biochem J. 1995 Dec 1;312 ( Pt 2):357-65
Authors: Mayo KH, Ilyina E, Roongta V, Dundas M, Joseph J, Lai CK, Maione T, Daly TJ
Native platelet factor-4 (PF4) is an...
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Biochemistry. 1994 Jan 11;33(1):65-73
Authors: Yamasaki K, Shirouzu M, Muto Y, Fujita-Yoshigaki J, Koide H, Ito Y, Kawai G, Hattori S, Yokoyama S, Nishimura S
The Tyr residues in positions 32 and 40 of human c-Ha-Ras...
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Biochemistry. 1994 Jan 11;33(1):65-73
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The Tyr residues in positions 32 and 40 of human c-Ha-Ras...
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Biochemistry. 1994 Dec 27;33(51):15298-308
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Flavodoxins mediate electron transfer at low redox...
Molecular analysis of sialoside binding to sialoadhesin by NMR and site-directed muta
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