Galactose-binding lectin: Difference between revisions

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**[[1l7l]], [[1uoj]] – GBL <br />
**[[1l7l]], [[1uoj]] – GBL <br />
**[[4cp9]], [[4cpb]], [[7z62]], [[7z63]] – GBL + galactoside <br />
**[[7fio]], [[7fjh]] – GBL + inhibitor<br />


*''PaGBL binary complex''
*''PaGBL binary complex''
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**[[2zqo]] – eGBL C-terminal + GalNac<br />
**[[2zqo]] – eGBL C-terminal + GalNac<br />
**[[6yf6]] – GBL C-terminal + fucoside derivative – ''Enterobacter cloacae''<br />
**[[6yf6]] – GBL C-terminal + fucoside derivative – ''Enterobacter cloacae''<br />
**[[6bfm]] – GBL - mussell<br />
**[[5vbk]], [[6bfm]] – GBL - mussell<br />
}}
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 14:07, 7 March 2023


Function

Galactose-binding lectin (GBL) is a lectin which binds the carbohydrate sequence Gal-β(1,3)-GalNac. GBL is an all beta-sheet protein[1].

Relevance

GBL is used in affinity columns for capturing proteins which are glycosylated with Gal-β(1,3)-GalNac.

Structural highlights

The carbohydrate ligand binds to 3 loops[2]. in peanut galactose-binding lectin (PDB entry 1v6i).

.

. Water molecules shown as red spheres.

Structure of peanut galactose-binding lectin tetramer complex with β-D-galactose, α-D-glucose, Ca+2 (green) and Mn+2 (purple) ions (PDB entry 1v6i)

Drag the structure with the mouse to rotate

3D structures of galactose-binding lectin3D structures of galactose-binding lectin

Updated on 07-March-2023

ReferencesReferences

  1. Natchiar SK, Srinivas O, Mitra N, Surolia A, Jayaraman N, Vijayan M. Structural studies on peanut lectin complexed with disaccharides involving different linkages: further insights into the structure and interactions of the lectin. Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1413-21. Epub 2006, Oct 18. PMID:17057347 doi:10.1107/S0907444906035712
  2. Kundhavai Natchiar S, Arockia Jeyaprakash A, Ramya TN, Thomas CJ, Suguna K, Surolia A, Vijayan M. Structural plasticity of peanut lectin: an X-ray analysis involving variation in pH, ligand binding and crystal structure. Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):211-9. Epub 2004, Jan 23. PMID:14747696 doi:http://dx.doi.org/10.1107/S090744490302849X

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky