To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https
PROSITE documentation PDOC00279

Galactoside-binding lectin (galectin) domain profile





Description

Galectins (also known as galaptins or S-lectin) are a family of proteins defined by having at least one characteristic carbohydrate recognition domain (CRD) with an affinity for β-galactosides and sharing certain sequence elements. Members of the galectins family are found in mammals, birds, amphibians, fish, nematodes, sponges, and some fungi. Galectins are known to carry out intra- and extracellular functions through glycoconjugate-mediated recogntion. From the cytosol they may be secreted by non-classical pathways, but they may also be targeted to the nucleus or specific sub-cytosolic sites. Within the same peptide chain some galectins have a CRD with only a few additional amino acids, whereas others have two CRDs joined by a link peptide, and one (galectin-3) has one CRD joined to a different type of domain [1,2,3].

The galectin carbohydrate recognition domain (CRD) is a β-sandwich of about 135 amino acid (see <PDB:1HLC>). The two sheets are slightly bent with 6 strands forming the concave side and 5 strands forming the convex side. The concave side forms a groove in which carbohydrate is bound, and which is long enough to hold about a linear tetrasaccharide [1,2,3,4,5].

A number of proteins are known to belong to this family:

  • Galectin-3 (also known as MAC-2 antigen; CBP-35 or IgE-binding protein), a 35 Kd lectin which binds immunoglobulin E and which is composed of two domains: a N-terminal domain that consist of tandem repeats of a glycine/ proline-rich sequence and a C-terminal galectin domain.
  • Galectin-4 [6], which is composed of two galectin domains.
  • Galectin-5.
  • Galectin-7 [7], a keratinocyte protein which could be involved in cell-cell and/or cell-matrix interactions necessary for normal growth control.
  • Galectin-8 [8], which is composed of two galectin domains.
  • Galectin-9 [9], which is composed of two galectin domains.
  • Human eosinophil lysophospholipase (EC 3.1.1.5) [5] (Charcot-Leyden crystal protein), a protein that may have both an enzymatic and a lectin activities. It forms hexagonal bipyramidal crystals in tissues and secretions from sites of eosinophil-associated inflammation.
  • Caenorhabditis elegans 32 Kd lactose-binding lectin [10]. This lectin is composed of two galectin domains.
  • Caenorhabditis elegans lec-7 and lec-8.

The profile we developed covers the entire galectin domain.

Last update:

March 2007 / Pattern removed, profile added and text revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

GALECTIN, PS51304; Galactoside-binding lectin (galectin) domain profile  (MATRIX)


References

1AuthorsLeffler H.
TitleIntroduction to galectins.;
SourceTrends Glycosci. Glycotechnol. 9:9-19(1997).

2AuthorsLeffler H., Carlsson S., Hedlund M., Qian Y., Poirier F.
TitleIntroduction to galectins.
SourceGlycoconj. J. 19:433-440(2004).
PubMed ID14758066
DOI10.1023/B:GLYC.0000014072.34840.04

3AuthorsBan M., Yoon H.-J., Demirkan E., Utsumi S., Mikami B., Yagi F.
TitleStructural basis of a fungal galectin from Agrocybe cylindracea for recognizing sialoconjugate.
SourceJ. Mol. Biol. 351:695-706(2005).
PubMed ID16051274
DOI10.1016/j.jmb.2005.06.045

4AuthorsLobsanov Y.D., Gitt M.A., Leffler H., Barondes S.H., Rini J.M.
TitleX-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution.
SourceJ. Biol. Chem. 268:27034-27038(1993).
PubMed ID8262940

5AuthorsLeonidas D.D., Elbert B.L., Zhou Z., Leffler H., Ackerman S.J., Acharya K.R.
TitleCrystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins.
SourceStructure 3:1379-1393(1995).
PubMed ID8747464

6AuthorsOda Y., Herrmann J., Gitt M.A., Turck C.W., Burlingame A.L., Barondes S.H., Leffler H.
TitleSoluble lactose-binding lectin from rat intestine with two different carbohydrate-binding domains in the same peptide chain.
SourceJ. Biol. Chem. 268:5929-5939(1993).
PubMed ID8449956

7AuthorsMadsen P., Rasmussen H.H., Flint T., Gromov P., Kruse T.A., Honore B., Vorum H., Celis J.E.
TitleCloning, expression, and chromosome mapping of human galectin-7.
SourceJ. Biol. Chem. 270:5823-5829(1995).
PubMed ID7534301

8AuthorsHadari Y.R., Paz K., Dekel R., Mestrovic T., Accili D., Zick Y.
TitleGalectin-8. A new rat lectin, related to galectin-4.
SourceJ. Biol. Chem. 270:3447-3453(1995).
PubMed ID7852431

9AuthorsWada J., Kanwar Y.S.
TitleIdentification and characterization of galectin-9, a novel beta-galactoside-binding mammalian lectin.
SourceJ. Biol. Chem. 272:6078-6086(1997).
PubMed ID9038233

10AuthorsHirabayashi J., Satoh M., Kasai K.-I.
TitleEvidence that Caenorhabditis elegans 32-kDa beta-galactoside-binding protein is homologous to vertebrate beta-galactoside-binding lectins. cDNA cloning and deduced amino acid sequence.
SourceJ. Biol. Chem. 267:15485-15490(1992).
PubMed ID1639789

11AuthorsAbbott W.M., Feizi T.
SourceJ. Biol. Chem. 266:5552-5557(1991).



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)