Galectin

Function

Galectin or galactoside-binding soluble lectin (GAL) are lectins which bind β-galactosidase (BGAL). GAL contains a carbohydrate recognition domain (CRD) residues 113-250^[1].

GAL-1 is thought to play a role as autocrine negative growth factor that regulates cell proliferation.
GAL-2 is expressed primarily in gastrointestinal tract.
GAL-3 has broad biological functionality.
GAL-4 has 2 CRDs.
GAL-5 is found in rat is a β-galactoside binding lectin^[2].
GAL-7 is associated with epithelial cells.
GAL-8 has a role in cellular defense against bacterial infection and vacuolar damage.
GAL-9 affects eosinophil survival.
GAL-10 or Charcot-Leyden crystal protein acts on biological membranes to regulate the multifunctional lysophospholipids.
GAL-13 is a placental protein which does not bind β-galactosides.

Relevance

GAL are known to inhibit chronic inflammation^[3]. GAL-3 has a role in experimental autoimmune encephalomyelitis and melanoma methastasis^[4].

Structural highlights

The CRD is a β-sandwich long enough to bind a tetrasaccharide. A ^[5]. Water molecules shown as red spheres.

3D structures of galectin

Galectin 3D structures

Structure of human galectin-1 complex with lactose, mercaptoethanol and sulfate (PDB entry 1w6o)

Drag the structure with the mouse to rotate

ReferencesReferences

↑ Barondes SH, Cooper DN, Gitt MA, Leffler H. Galectins. Structure and function of a large family of animal lectins. J Biol Chem. 1994 Aug 19;269(33):20807-10. PMID:8063692
↑ Barres C, Blanc L, Bette-Bobillo P, Andre S, Mamoun R, Gabius HJ, Vidal M. Galectin-5 is bound onto the surface of rat reticulocyte exosomes and modulates vesicle uptake by macrophages. Blood. 2010 Jan 21;115(3):696-705. doi: 10.1182/blood-2009-07-231449. Epub 2009, Nov 10. PMID:19903899 doi:http://dx.doi.org/10.1182/blood-2009-07-231449
↑ Liu FT, Rabinovich GA. Galectins: regulators of acute and chronic inflammation. Ann N Y Acad Sci. 2010 Jan;1183:158-82. doi: 10.1111/j.1749-6632.2009.05131.x. PMID:20146714 doi:http://dx.doi.org/10.1111/j.1749-6632.2009.05131.x
↑ Radosavljevic G, Volarevic V, Jovanovic I, Milovanovic M, Pejnovic N, Arsenijevic N, Hsu DK, Lukic ML. The roles of Galectin-3 in autoimmunity and tumor progression. Immunol Res. 2012 Apr;52(1-2):100-10. doi: 10.1007/s12026-012-8286-6. PMID:22418727 doi:http://dx.doi.org/10.1007/s12026-012-8286-6
↑ Lopez-Lucendo MF, Solis D, Andre S, Hirabayashi J, Kasai K, Kaltner H, Gabius HJ, Romero A. Growth-regulatory human galectin-1: crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding. J Mol Biol. 2004 Oct 29;343(4):957-70. PMID:15476813 doi:http://dx.doi.org/10.1016/j.jmb.2004.08.078

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

Michal Harel, Alexander Berchansky, Joel L. Sussman

[1] Barondes SH, Cooper DN, Gitt MA, Leffler H. Galectins. Structure and function of a large family of animal lectins. J Biol Chem. 1994 Aug 19;269(33):20807-10. PMID:8063692

[2] Barres C, Blanc L, Bette-Bobillo P, Andre S, Mamoun R, Gabius HJ, Vidal M. Galectin-5 is bound onto the surface of rat reticulocyte exosomes and modulates vesicle uptake by macrophages. Blood. 2010 Jan 21;115(3):696-705. doi: 10.1182/blood-2009-07-231449. Epub 2009, Nov 10. PMID:19903899 doi:http://dx.doi.org/10.1182/blood-2009-07-231449

[3] Liu FT, Rabinovich GA. Galectins: regulators of acute and chronic inflammation. Ann N Y Acad Sci. 2010 Jan;1183:158-82. doi: 10.1111/j.1749-6632.2009.05131.x. PMID:20146714 doi:http://dx.doi.org/10.1111/j.1749-6632.2009.05131.x

[4] Radosavljevic G, Volarevic V, Jovanovic I, Milovanovic M, Pejnovic N, Arsenijevic N, Hsu DK, Lukic ML. The roles of Galectin-3 in autoimmunity and tumor progression. Immunol Res. 2012 Apr;52(1-2):100-10. doi: 10.1007/s12026-012-8286-6. PMID:22418727 doi:http://dx.doi.org/10.1007/s12026-012-8286-6

[5] Lopez-Lucendo MF, Solis D, Andre S, Hirabayashi J, Kasai K, Kaltner H, Gabius HJ, Romero A. Growth-regulatory human galectin-1: crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding. J Mol Biol. 2004 Oct 29;343(4):957-70. PMID:15476813 doi:http://dx.doi.org/10.1016/j.jmb.2004.08.078

[1]

[2]

[3]

[4]

[5]

Galectin

Contents

Function

Relevance

Structural highlights

3D structures of galectin

ReferencesReferences

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

Navigation menu

Galectin

Function

Relevance

Structural highlights

3D structures of galectin

ReferencesReferences

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

Navigation menu

Search