Curr Opin Struct Biol. 1999 Dec;9(6):707-14.

Lectins.

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Molecular Biophysics Unit, Indian Institute of Science, Bangalore, 560 012, India. mv@mbu.iisc.ernet.in

Abstract

Lectins - carbohydrate-binding proteins involved in a variety of recognition processes - exhibit considerable structural diversity. Three new lectin folds and further elaborations of known folds have been described recently. Large variability in quaternary association resulting from small alterations in essentially the same tertiary structure is a property exhibited specially by legume lectins. The strategies used by lectins to generate carbohydrate specificity include the extensive use of water bridges, post-translational modification and oligomerization. Recent results pertaining to influenza and foot-and-mouth viruses further elaborate the role of lectins in infection.

PMID:: 10607664; [PubMed - indexed for MEDLINE]

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Lectins

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Carbohydrate specificity and quaternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 A resolution. [J Mol Biol. 1998]
Carbohydrate specificity and quaternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 A resolution.
Prabu MM, Sankaranarayanan R, Puri KD, Sharma V, Surolia A, Vijayan M, Suguna K. J Mol Biol. 1998 Mar 6; 276(4):787-96.
Structural basis of carbohydrate recognition by lectin II from Ulex europaeus, a protein with a promiscuous carbohydrate-binding site. [J Mol Biol. 2000]
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. 2000 Aug 25; 301(4):987-1002.
Review Insights into the quaternary association of proteins through structure graphs: a case study of lectins. [Biochem J. 2005]
Review Insights into the quaternary association of proteins through structure graphs: a case study of lectins.
Brinda KV, Surolia A, Vishveshwara S. Biochem J. 2005 Oct 1; 391(Pt 1):1-15.
Variability in quaternary association of proteins with the same tertiary fold: a case study and rationalization involving legume lectins. [Proteins. 1999]
Variability in quaternary association of proteins with the same tertiary fold: a case study and rationalization involving legume lectins.
Prabu MM, Suguna K, Vijayan M. Proteins. 1999 Apr 1; 35(1):58-69.
Review Legume lectin family, the 'natural mutants of the quaternary state', provide insights into the relationship between protein stability and oligomerization. [Biochim Biophys Acta. 2001]
Review Legume lectin family, the 'natural mutants of the quaternary state', provide insights into the relationship between protein stability and oligomerization.
Srinivas VR, Reddy GB, Ahmad N, Swaminathan CP, Mitra N, Surolia A. Biochim Biophys Acta. 2001 Aug 15; 1527(3):102-11.

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Cited by 16 PubMed Central articles

AnimalLectinDb: An integrated animal lectin database. [Bioinformation. 2011]
AnimalLectinDb: An integrated animal lectin database.
Kumar D, Mittal Y. Bioinformation. 2011; 6(3):134-6. Epub 2011 Apr 22.
Analysis and prediction of cancerlectins using evolutionary and domain information. [BMC Res Notes. 2011]
Analysis and prediction of cancerlectins using evolutionary and domain information.
Kumar R, Panwar B, Chauhan JS, Raghava GP. BMC Res Notes. 2011 Jul 20; 4:237. Epub 2011 Jul 20.
Functional alteration of a dimeric insecticidal lectin to a monomeric antifungal protein correlated to its oligomeric status. [PLoS One. 2011]
Functional alteration of a dimeric insecticidal lectin to a monomeric antifungal protein correlated to its oligomeric status.
Banerjee N, Sengupta S, Roy A, Ghosh P, Das K, Das S. PLoS One. 2011 Apr 7; 6(4):e18593. Epub 2011 Apr 7.

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