A minimized human insulin-receptor-binding motif revealed in a Conus geographus venom insulin

Nature Structural and Molecular Biology

Volumn 23, Issue 10, 2016, Pages 916-920

  Menting, John G ^a   Gajewiak, Joanna ^b   MacRaild, Christopher A ^c   Chou, Danny Hung Chieh ^d   Disotuar, Maria M ^d   Smith, Nicholas A ^e   Miller, Charleen ^f   Erchegyi, Judit ^f   Rivier, Jean E ^f   Olivera, Baldomero M ^b   Forbes, Briony E ^g   Smith, Brian J ^e   Norton, Raymond S ^c   Safavi Hemami, Helena ^b,h   Lawrence, Michael C ^a,i  

^a WALTER AND ELIZA HALL INSTITUTE OF MEDICAL RESEARCH   (Australia)

^b UNIVERSITY OF UTAH   (United States)

^c MONASH UNIVERSITY   (Australia)

^d UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

^e LA TROBE UNIVERSITY   (Australia)

^f Sentia Medical Sciences   (United States)

^g FLINDERS UNIVERSITY   (Australia)

^h UNIVERSITY OF COPENHAGEN   (Denmark)

ⁱ UNIVERSITY OF MELBOURNE   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

HUMAN INSULIN; INSULIN RECEPTOR; SELENOCYSTEINE; VENOM; INSR PROTEIN, HUMAN; INSULIN; LEUKOCYTE ANTIGEN; PROTEIN BINDING;

AMINO ACID SYNTHESIS; ARTICLE; CONTROLLED STUDY; CONUS GEOGRAPHUS; CRYSTALLIZATION; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTEIN STRUCTURE; RECEPTOR AFFINITY; RECEPTOR BINDING; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; CONUS (SNAIL); HUMAN; METABOLISM; MOLECULAR MODEL; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION;

AMINO ACID SEQUENCE; ANIMALS; ANTIGENS, CD; CONUS SNAIL; HUMANS; INSULIN; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; RECEPTOR, INSULIN; SELENOCYSTEINE; VENOMS;

EID: 84987624996     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.3292     Document Type: Article

References (31)

1. King, G.F. Venoms as a platform for human drugs: translating toxins into therapeutics. Expert Opin. Biol. Ther. 11, 1469-1484 (2011).
2. Zambelli, V.O., Pasqualoto, K.F., Picolo, G., Chudzinski-Tavassi, A.M., Cury, Y. Harnessing the knowledge of animal toxins to generate drugs. Pharmacol. Res. http://dx.doi.org/10.1016/j.phrs.2016.01.009 (2016).
3. Safavi-Hemami, H. et al. Specialized insulin is used for chemical warfare by fish-hunting cone snails. Proc. Natl. Acad. Sci. USA 112, 1743-1748 (2015).
4. Adams, M.J. et al. Structure of rhombohedral 2 zinc insulin crystals. Nature 224, 491-495 (1969).
5. Owens, D.R. New horizons: alternative routes for insulin therapy. Nat. Rev. Drug Discov. 1, 529-540 (2002).
6. Bao, S.J., Xie, D.L., Zhang, J.P., Chang, W.R., Liang, D.C. Crystal structure of desheptapeptide(B24-B30)insulin at 1.6 A resolution: implications for receptor binding. Proc. Natl. Acad. Sci. USA 94, 2975-2980 (1997).
7. Walewska, A. et al. Integrated oxidative folding of cysteine/selenocysteine containing peptides: improving chemical synthesis of conotoxins. Angew. Chem. Int. Edn. Engl. 48, 2221-2224 (2009).
8. Denley, A. et al. Structural determinants for high-affinity binding of insulin-like growth factor II to insulin receptor (IR)-A, the exon 11 minus isoform of the IR. Mol. Endocrinol. 18, 2502-2512 (2004).
9. Timofeev, V.I. et al. X-ray investigation of gene-engineered human insulin crystallized from a solution containing polysialic acid. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66, 259-263 (2010).
10. Weiss, M.A. The structure and function of insulin: decoding the TR transition. Vitam. Horm. 80, 33-49 (2009).
11. Menting, J.G. et al. How insulin engages its primary binding site on the insulin receptor. Nature 493, 241-245 (2013).
12. Menting, J.G. et al. Protective hinge in insulin opens to enable its receptor engagement. Proc. Natl. Acad. Sci. USA 111, E3395-E3404 (2014).
13. Muttenthaler, M., Ramos, Y.G., Feytens, D., de Araujo, A.D., Alewood, P.F. p-Nitrobenzyl protection for cysteine and selenocysteine: a more stable alternative to the acetamidomethyl group. Biopolymers 94, 423-432 (2010).
14. Smith, G.D., Pangborn, W.A., Blessing, R.H. The structure of T6 human insulin at 1.0 A resolution. Acta Crystallogr. D Biol. Crystallogr. 59, 474-482 (2003).
15. Rivier, J. et al. Total synthesis and further characterization of the ?-carboxyglutamate-containing "sleeper" peptide from Conus geographus venom. Biochemistry 26, 8508-8512 (1987).
16. Galande, A.K., Weissleder, R., Tung, C.-H. An effective method of on-resin disulfide bond formation in peptides. J. Comb. Chem. 7, 174-177 (2005).
17. Houtman, J.C. et al. Studying multisite binary and ternary protein interactions by global analysis of isothermal titration calorimetry data in SEDPHAT: application to adaptor protein complexes in cell signaling. Protein Sci. 16, 30-42 (2007).
18. Laue, T., Shah, D., Ridgeway, T., Pelletier, S. in Analytical Ultracentrifugation in Biochemistry and Polymer Science (eds. Harding, S., Rowe, A.J., Horton, J.C.) 90-125 (Royal Society of Chemistry, 1992).
19. Dai, Q., Dong, M., Liu, Z., Prorok, M., Castellino, F.J. Ca 2+-induced self-assembly in designed peptides with optimally spaced ?-carboxyglutamic acid residues. J. Inorg. Biochem. 105, 52-57 (2011).
20. Cnudde, S.E., Prorok, M., Jia, X., Castellino, F.J., Geiger, J.H. The crystal structure of the calcium-bound con-G[Q6A] peptide reveals a novel metal-dependent helical trimer. J. Biol. Inorg. Chem. 16, 257-266 (2011).
21. Chen, Z. et al. Conformational changes in conantokin-G induced upon binding of calcium and magnesium as revealed by NMR structural analysis. J. Biol. Chem. 273, 16248-16258 (1998).
22. Kabsch, W. Integration, scaling, space-group assignment and post-refinement. Acta Crystallogr. D Biol. Crystallogr. 66, 133-144 (2010).
23. McCoy, A.J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
24. Adams, P.D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
25. Emsley, P., Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132 (2004).
26. Webb, B., Sali, A. Comparative protein structure modeling using MODELLER. Curr. Protoc. Bioinformatics 47, 5-6 (2014).
27. Hua, Q.X. et al. Structure of a protein in a kinetic trap. Nat. Struct. Biol. 2, 129-138 (1995).
28. Sparrow, L.G. et al. N-linked glycans of the human insulin receptor and their distribution over the crystal structure. Proteins 71, 426-439 (2008).
29. Pronk, S. et al. GROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit. Bioinformatics 29, 845-854 (2013).
30. Guvench, O. et al. CHARMM additive all-atom force field for carbohydrate derivatives and its utility in polysaccharide and carbohydrate-protein modeling. J. Chem. Theory Comput. 7, 3162-3180 (2011).
31. Best, R.B. et al. Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone ?, ? and side-chain ?(1) and ?(2) dihedral angles. J. Chem. Theory Comput. 8, 3257-3273 (2012).