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The role of weak protein-protein interactions in multivalent lectin-carbohydrate binding: crystal structure of cross-linked FRIL.

Hamelryck TW, Moore JG, Chrispeels MJ, Loris R, Wyns L
J Mol Biol 299 875-83 (2000)
Cited: 31 times
EuropePMC logo PMID: 10843844

Abstract

Binding of multivalent glycoconjugates by lectins often leads to the formation of cross-linked complexes. Type I cross-links, which are one-dimensional, are formed by a divalent lectin and a divalent glycoconjugate. Type II cross-links, which are two or three-dimensional, occur when a lectin or glycoconjugate has a valence greater than two. Type II complexes are a source of additional specificity, since homogeneous type II complexes are formed in the presence of mixtures of lectins and glycoconjugates. This additional specificity is thought to become important when a lectin interacts with clusters of glycoconjugates, e.g. as is present on the cell surface. The cryst1al structure of the Glc/Man binding legume lectin FRIL in complex with a trisaccharide provides a molecular snapshot of how weak protein-protein interactions, which are not observed in solution, can become important when a cross-linked complex is formed. In solution, FRIL is a divalent dimer, but in the crystal FRIL forms a tetramer, which allows for the formation of an intricate type II cross-linked complex with the divalent trisaccharide. The dependence on weak protein-protein interactions can ensure that a specific type II cross-linked complex and its associated specificity can occur only under stringent conditions, which explains why lectins are often found forming higher-order oligomers.

Reviews - 1qmo mentioned but not cited (1)

  1. Research advances and prospects of legume lectins. Katoch R, Tripathi A. J Biosci 46 104 (2021)

Articles - 1qmo mentioned but not cited (5)

  1. Energetics of galactose- and glucose-aromatic amino acid interactions: implications for binding in galactose-specific proteins. Sujatha MS, Sasidhar YU, Balaji PV. Protein Sci 13 2502-2514 (2004)
  2. Crystallization and preliminary X-ray crystallographic analysis of a galactose-specific lectin from Dolichos lablab. Latha VL, Kulkarni KA, Rao RN, Kumar NS, Suguna K. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 163-165 (2006)
  3. Automated identification of protein-ligand interaction features using Inductive Logic Programming: a hexose binding case study. A Santos JC, Nassif H, Page D, Muggleton SH, E Sternberg MJ. BMC Bioinformatics 13 162 (2012)
  4. A Carbohydrate-Binding Protein from the Edible Lablab Beans Effectively Blocks the Infections of Influenza Viruses and SARS-CoV-2. Liu YM, Shahed-Al-Mahmud M, Chen X, Chen TH, Liao KS, Lo JM, Wu YM, Ho MC, Wu CY, Wong CH, Jan JT, Ma C. Cell Rep 32 108016 (2020)
  5. An Inductive Logic Programming Approach to Validate Hexose Binding Biochemical Knowledge. Nassif H, Al-Ali H, Khuri S, Keirouz W, Page D. Inductive Log Program 5989 149-165 (2010)


Reviews citing this publication (2)

  1. Glycohistochemistry: the why and how of detection and localization of endogenous lectins. Gabius HJ. Anat Histol Embryol 30 3-31 (2001)
  2. Cell-Inspired All-Aqueous Microfluidics: From Intracellular Liquid-Liquid Phase Separation toward Advanced Biomaterials. Ma Q, Song Y, Sun W, Cao J, Yuan H, Wang X, Sun Y, Shum HC. Adv Sci (Weinh) 7 1903359 (2020)

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  1. Crystal contacts as nature's docking solutions. Krissinel E. J Comput Chem 31 133-143 (2010)
  2. Functional sites in protein families uncovered via an objective and automated graph theoretic approach. Wangikar PP, Tendulkar AV, Ramya S, Mali DN, Sarawagi S. J. Mol. Biol. 326 955-978 (2003)
  3. An amino acid has two sides: a new 2D measure provides a different view of solvent exposure. Hamelryck T. Proteins 59 38-48 (2005)
  4. Determinants of quaternary association in legume lectins. Brinda KV, Mitra N, Surolia A, Vishveshwara S. Protein Sci. 13 1735-1749 (2004)
  5. Native crystal structure of a nitric oxide-releasing lectin from the seeds of Canavalia maritima. Gadelha CA, Moreno FB, Santi-Gadelha T, Cajazeiras JB, Rocha BA, Assreuy AM, Lima Mota MR, Pinto NV, Passos Meireles AV, Borges JC, Freitas BT, Canduri F, Souza EP, Delatorre P, Criddle DN, de Azevedo WF, Cavada BS. J. Struct. Biol. 152 185-194 (2005)
  6. Structural basis of oligomannose recognition by the Pterocarpus angolensis seed lectin. Loris R, Van Walle I, De Greve H, Beeckmans S, Deboeck F, Wyns L, Bouckaert J. J. Mol. Biol. 335 1227-1240 (2004)
  7. Structural basis of carbohydrate recognition by lectin II from Ulex europaeus, a protein with a promiscuous carbohydrate-binding site. Loris R, De Greve H, Dao-Thi MH, Messens J, Imberty A, Wyns L. J. Mol. Biol. 301 987-1002 (2000)
  8. Weak protein-protein interactions in lectins: the crystal structure of a vegetative lectin from the legume Dolichos biflorus. Buts L, Dao-Thi MH, Loris R, Wyns L, Etzler M, Hamelryck T. J. Mol. Biol. 309 193-201 (2001)
  9. Three-dimensional structure of the lithostathine protofibril, a protein involved in Alzheimer's disease. Grégoire C, Marco S, Thimonier J, Duplan L, Laurine E, Chauvin JP, Michel B, Peyrot V, Verdier JM. EMBO J. 20 3313-3321 (2001)
  10. Similarity between protein-protein and protein-carbohydrate interactions, revealed by two crystal structures of lectins from the roots of pokeweed. Hayashida M, Fujii T, Hamasu M, Ishiguro M, Hata Y. J. Mol. Biol. 334 551-565 (2003)
  11. Purification of a PHA-like chitin-binding protein from Acacia farnesiana seeds: a time-dependent oligomerization protein. Santi-Gadelha T, Rocha BA, Oliveira CC, Aragão KS, Marinho ES, Gadelha CA, Toyama MH, Pinto VP, Nagano CS, Delatorre P, Martins JL, Galvani FR, Sampaio AH, Debray H, Cavada BS. Appl. Biochem. Biotechnol. 150 97-111 (2008)
  12. Structural basis for the recognition of complex-type biantennary oligosaccharides by Pterocarpus angolensis lectin. Buts L, Garcia-Pino A, Imberty A, Amiot N, Boons GJ, Beeckmans S, Versées W, Wyns L, Loris R. FEBS J. 273 2407-2420 (2006)
  13. Multivalent mannose-displaying nanoparticles constructed from poly{styrene-co-[(maleic anhydride)-alt-styrene]}. Su R, Li L, Chen X, Han J, Han S. Org. Biomol. Chem. 7 2040-2045 (2009)
  14. Purification, characterization, and preliminary X-ray diffraction analysis of a lactose-specific lectin from Cymbosema roseum seeds. Rocha BA, Moreno FB, Delatorre P, Souza EP, Marinho ES, Benevides RG, Rustiguel JK, Souza LA, Nagano CS, Debray H, Sampaio AH, de Azevedo WF, Cavada BS. Appl. Biochem. Biotechnol. 152 383-393 (2009)
  15. N-glycan analysis of mannose/glucose specific lectin from Dolichos lablab seeds. B S GK, Pohlentz G, Schulte M, Mormann M, Nadimpalli SK. Int. J. Biol. Macromol. 69 400-407 (2014)
  16. Affinity of a galactose-specific legume lectin from Dolichos lablab to adenine revealed by X-ray cystallography. Shetty KN, Latha VL, Rao RN, Nadimpalli SK, Suguna K. IUBMB Life 65 633-644 (2013)
  17. Effects of Canavalia lectins on acute inflammation in sensitized and non-sensitized rats. Pinto NV, Cavada BS, Brito LF, Pereira RI, da Silva MT, Castro RR, de Freitas Pires A, Assreuy AM. Inflammation 36 713-722 (2013)
  18. Legume lectin FRIL preserves neural progenitor cells in suspension culture in vitro. Yao H, Xie X, Li Y, Wang D, Han S, Shi S, Nan X, Bai C, Wang Y, Pei X. Clin. Dev. Immunol. 2008 531317 (2008)
  19. Molecular and functional characterization of a glycosylated Galactose-Binding lectin from Mytilus californianus. García-Maldonado E, Cano-Sánchez P, Hernández-Santoyo A. Fish Shellfish Immunol. 66 564-574 (2017)
  20. Structural basis of carbohydrate recognition by a Man(alpha1-2)Man-specific lectin from Bowringia milbraedii. Buts L, Garcia-Pino A, Wyns L, Loris R. Glycobiology 16 635-640 (2006)
  21. Molecular characterization of a wheat protein induced by vernalisation. Bertini L, Proietti S, Caporale C, Caruso C. Protein J. 28 253-262 (2009)
  22. Molecular modeling of lectin-like protein from Acacia farnesiana reveals a possible anti-inflammatory mechanism in Carrageenan-induced inflammation. Abrantes VE, Matias da Rocha BA, Batista da Nóbrega R, Silva-Filho JC, Teixeira CS, Cavada BS, Gadelha CA, Ferreira SH, Figueiredo JG, Santi-Gadelha T, Delatorre P. Biomed Res Int 2013 253483 (2013)
  23. Crystal structure of a Xenopus laevis skin proto-type galectin, close to but distinct from galectin-1. Nonaka Y, Ogawa T, Yoshida H, Shoji H, Nishi N, Kamitori S, Nakamura T. Glycobiology 25 792-803 (2015)


Related citations provided by authors (2)

  1. cDNA cloning of FRIL, a lectin from Dolichos lablab, that preserves hematopoietic progenitors in suspension culture.. Colucci G, Moore JG, Feldman M, Chrispeels MJ Proc Natl Acad Sci U S A 96 646-50 (1999)
  2. Purification and characterization of Dolichos lablab lectin.. Mo H, Meah Y, Moore JG, Goldstein IJ Glycobiology 9 173-9 (1999)

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