Unfolding energetics and stability of banana lectin

Proteins: Structure, Function and Genetics

Volumn 72, Issue 2, 2008, Pages 754-760

  Gupta, Garima ^a   Sinha, Sharmistha ^a   Surolia, Avadhesha ^a,b  

^a INDIAN INSTITUTE OF SCIENCE   (India)

^b NATIONAL INSTITUTE OF IMMUNOLOGY   (India)

Author keywords

Banana lectin (banlec); Chaotropic denaturation; Free energy G; Hydrogen bonds; Two state unfolding

Indexed keywords

PLANT LECTIN;

ARTICLE; BANANA; ENERGY TRANSFER; HYDROGEN BOND; HYDROPHOBICITY; NONHUMAN; PHYTOCHEMISTRY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY;

DIMERIZATION; GUANIDINE; HYDROGEN BONDING; LECTINS; MUSA; PROTEIN CONFORMATION; PROTEIN DENATURATION; TEMPERATURE;

MUSA X PARADISIACA;

EID: 46449121619     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21961     Document Type: Article

References (28)

1. Lis H, Sharon N. Lectins: Carbohydrate specific proteins that mediate cellular recognition. Chem Rev 1998;98:637-664.
2. Drickamer K. C-type lectin-like domains. Curr Opin Struct Biol 1999;9:585-590.
3. Vijayan M, Chandra N. Lectins. Curr Opin Struct Biol 1999;9:707-714.
4. Loris R. Principles of structures of animal and plant lectins. Biochim Biophys Acta 2002;1572:198-208.
5. Koshte VL, Dijk WV, Stelt MEVD, Aalberse RC. Isolation and characterization of Banlec-I, a mannoside-binding lectin from Musa paradisiaca (banana). Biochem J 1990;272:721-726.
6. Peumans WJ, Zhang W, Barre A, Houles-Astoul C, Balint-Kurti PL, Rovira P, Rouge P, May GD, Van Leuven F, Truffa-Bachi P, Van Damme EJ. Fruit-specific lectins from banana and plantain. Planta 2000;211:546-554.
7. Shankarnarayanan R, Sekar K, Banerjee R, Sharma V, Surolia A, Vijayan M. A novel mode of carbohydrate recognition in Jacalin, a Moraceae plant lectin with a β-prism fold. Nat Struct Biol 1996;3:596-603.
8. Pratap JV, Jeyaprakash AA, Rani PG, Sekar K, Surolia A, Vijayan M. Crystal structure of artocarpin, a Moraceae lectin with mannose specificity, and its complex with methyl-α-D-mannose: Implications to the generation of carbohydrate specificity. J Mol Biol 2002;317:237-247.
9. Bourne Y, Roig-Zamboni V, Barre A, Peumans WJ, Astoul CH, Van Dammer EJM, Rouge P. The crystal structure of the Calystegia sepium agglutinin reveals a novel quaternary arrangement of lectin subunits with a β-prism fold. J Biol Chem 2004;279:527-533.
10. Bourne Y, Zamboni V, Barre A, Peumans WJ, Van Damme EJM, Rouge P. Helianthus tuberosus lectin reveals a widespread scaffold for mannose-binding lectins. Structure 1999;7:1473-1482.
11. Mo H, Winter HC, Van Damme EJM, Peumans WJ, Misaki A, Goldstein IJ. Carbohydrate-binding properties of the banana (Musa acuminata) lectin. I. Novel recognition of internal α1,3-linked glucosyl residues. Eur J Biochem 2001;268:2609-2615.
12. Goldstein IJ, Winter HC, Mo H, Misaki A, Van Damme EJM, Peumans WJ. Carbohydrate-binding properties of the banana (Musa acuminata) lectin. II. Binding of laminaribiose oligosaccharide and β-glucans containing β1,6-linked glucosyl end groups. Eur J Biochem 2001;268:2616-2619.
13. Singh DD, Saikrishnan K, Kumar P, Surolia A, Sekar K, Vijayan M. Unusual sugar specificity of banana lectin from Musa paradisiaca and its probable evolutionary origin. Crystallographic and modelling studies. Glycobiology 2005;10:1025-1032.
14. Hester G, Kaku H, Goldstein IJ, Wright CS. Structure of mannose specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family. Nat Struc Biol 1995;2:472-479.
15. Clavel C, Canales A, Gupta G, Santos JI, Canada FJ, Penades S, Surolia A, Jimenez-Barbero J. NMR studies on the conformation of oligomannosides and their interaction with banana lectin. Glucoconj J 2007;24:449-464.
16. Clavel C, Canales A, Gupta G, Javier Canada F, Penades S, Surolia A, Jimenez-Barbero J. NMR investigation of the bound conformation of natural and synthetic oligomannosides to banana lectin. Eur J Org Chem 2007;10:1577-1585.
17. Pace CN. Conformational stability of globular proteins. Trends Biochem Sci 1990;15:14-17.
18. Barrick D, Baldwin RL. Stein and Moore Award address: The molten globule intermediate of apomyoglobin and the process of protein folding. Protein Sci 1993;2:869-876.
19. Gualfetti PJ, Bilsel O, Matthews CR. The progressive development of structure and stability during the equilibrium folding of the α subunit of tryptophan synthase from Escherichia coli. Protein Sci 1999;8:1623-1635.
20. Sinha S, Mitra N, Kumar G, Bajaj K, Surolia A. Unfolding studies on soybean agglutinin and concanavalin a tetramers: A comparative account. Biophys J 2005;88:1300-1310.
21. Schellman JA. Selective binding and solvent denaturation. Biophys Chem 1990;37:121-140.
22. Nicholson EM, Scholtz JM. Conformational stability of the Escherichia coli HPr protein: Test of the linear extrapolation method and a thermodynamic characterization of cold denaturation. Biochemistry 1996;35:11369-11378.
23. Agashe VR, Udgaonkar JB. Thermodynamics of denaturation of barstar: Evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride. Biochemistry 1995;34:3286-3299.
24. Bajaj K, Chakshusmathi G, Bachhawat-Sikder K, Surolia A, Varadarajan R. Thermodynamic characterization of monomeric and dimeric forms of CcdB (controller of cell division or death B protein). Biochem J 2004;380:409-417.
25. Neet KE, Timm DE. Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturation. Protein Sci 1994;3:2167-2174.
26. De Francesco R, Pastore A, Vecchio G, Cortese R. Circular dichroism study on the conformational stability of the dimerization of transcription factor LFB1. Biochemistry 1991;30:143-147.
27. Timm DE, deHaseth PL, Neet KE. Comparative equilibrium denaturation studies of the neurotrophins: NGF. BDNF, NT-3 and NT-4/5. Biochemistry 1994;33:4667-4676.
28. 2+ affinity, formation and stability of a two-site domain in troponin C. Protein Sci 1992;1:945-955.