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33 a.a.
Key reference
DOI no: 10.1021/bi983018j Biochemistry 38:8377-8384 (1999) PubMed id: 10387083
Effects of glycosylation on the structure and dynamics of eel calcitonin in micelles and lipid bilayers determined by nuclear magnetic resonance spectroscopy. Y.Hashimoto, K.Toma, J.Nishikido, K.Yamamoto, K.Haneda, T.Inazu, K.G.Valentine, S.J.Opella. ABSTRACT
The three-dimensional structures of eel calcitonin (CT) and two glycosylated CT derivatives, [Asn(GlcNAc)3]-CT (CT-GlcNAc) and [Asn(Man6-GlcNAc2)3]-CT (CT-M6), in micelles were determined by solution NMR spectroscopy. The topologies of these peptides associated with oriented lipid bilayers were determined with solid-state NMR. All of the peptides were found to have an identical conformation in micelles characterized by an amphipathic alpha-helix consisting of residues Ser5 through Leu19 followed by an unstructured region at the C-terminus. The overall conformation of the peptide moiety was not affected by the glycosylation. Nevertheless, comparison of the relative exchange rates of the Leu12 amide proton might suggest the possibility that fluctuations of the alpha-helix are reduced by glycosylation. The presence of NOEs between the carbohydrate and the peptide moieties of CT-GlcNAc and CT-M6 and the amide proton chemical shift data suggested that the carbohydrate interacted with the peptide, and this might account for the conformational stabilization of the alpha-helix. Both the unmodified CT and the glycosylated CT were found to have orientations with their helix axes parallel to the plane of the lipid bilayers by solid-state NMR spectroscopy.
Literature references that cite this PDB file's key reference
PubMed id Reference
19690964 L.Skrisovska, M.Schubert, and F.H.Allain (2010).
Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins.J Biomol NMR, 46, 51-65.
18835893 R.Høiberg-Nielsen, P.Westh, and L.Arleth (2009).
The effect of glycosylation on interparticle interactions and dimensions of native and denatured phytase.Biophys J, 96, 153-161.
17033777 H.A.Scheidt, A.Vogel, A.Eckhoff, B.W.Koenig, and D.Huster (2007).
Solid-state NMR characterization of the putative membrane anchor of TWD1 from Arabidopsis thaliana.Eur Biophys J, 36, 393-404.
15929987 V.Pham, M.Dong, J.D.Wade, L.J.Miller, C.J.Morton, H.L.Ng, M.W.Parker, and P.M.Sexton (2005).
Insights into interactions between the alpha-helical region of the salmon calcitonin antagonists and the human calcitonin receptor using photoaffinity labeling.J Biol Chem, 280, 28610-28622.
11948441 L.Stella, M.Venanzi, M.Carafa, E.Maccaroni, M.E.Straccamore, G.Zanotti, A.Palleschi, and B.Pispisa (2002).
Structural features of model glycopeptides in solution and in membrane phase: a spectroscopic and molecular mechanics investigation.Biopolymers, 64, 44-56.
11579442 D.F.Mierke, and C.Giragossian (2001).
Peptide hormone binding to G-protein-coupled receptors: structural characterization via NMR techniques.Med Res Rev, 21, 450-471.
16233137 K.Yamamoto (2001).
Chemo-enzymatic synthesis of bioactive glycopeptide using microbial endoglycosidase.J Biosci Bioeng, 92, 493-501.
11720996 V.Stipani, E.Gallucci, S.Micelli, V.Picciarelli, and R.Benz (2001).
Channel formation by salmon and human calcitonin in black lipid membranes.Biophys J, 81, 3332-3338. The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.
