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PROSITE documentation PDOC51752

Jacalin-type lectin domain profile





Description

Lectins, a well-known class of carbohydrate-binding proteins, are known to be important in a variety of biological processes, mediated through their carbohydrate specificities. Plant lectins are broadly divided into six classes based on their subunit folds. These are legume lectins (see <PDOC00278>), jacalin-related lectins (JRLs), monocot mannose-binding lectins (see <PDOC50927>), trefoil lectins, cyanovirin-N lectin, and hevein domain lectins. JRLs derive their name from jacalin, the first member to be identified from the seed of jackfruit. Based on the known sugar specificities, lectins in this family can be broadly divided into two classes: (1) the galactose-specific lectins and (2) the mannose/glucose-specific lectins [1,2,3,4,5].

The ~135-150 amino acid residue jacalin-type lectin domain adopts a β-prism-I fold comprised of three Greek keys (four stranded β-sheets) (see <PDB:3APA>) [4].

Some proteins known to contain a jacalin-type lectin domain are listed below:

  • Artocarpus integrifolia (jackfruit) jacalin.
  • Artocarpus ntegrifolia (jackfruit) artocarpin.
  • Morus nigra (black mulberry) mornigaG and mornigaM.
  • Ipomoea batatas (sweet potato) ipomoelin (IPO).
  • Musa acuminata (banana) lectin BanLec.
  • Helianthus tuberosus (Jerusalem artichoke) Heltuba.
  • Griffithsia sp. griffithsin.
  • Mammalian zymogen granule membrane protein 16 (ZG16) and zymogen granule protein 16 homolog B (ZG16b).

The profile we developed covers the entire jacalin-type lectin domain.

Last update:

March 2015 / First entry.

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Technical section

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

JACALIN_LECTIN, PS51752; Jacalin-type lectin domain profile  (MATRIX)


References

1AuthorsRaval S. Gowda S.B. Singh D.D. Chandra N.R.
TitleA database analysis of jacalin-like lectins: sequence-structure-function relationships.
SourceGlycobiology 14:1247-1263(2004).
PubMed ID15329359
DOI10.1093/glycob/cwh140

2AuthorsRabijns A. Barre A. Van Damme E.J.M. Peumans W.J. De Ranter C.J. Rouge P.
TitleStructural analysis of the jacalin-related lectin MornigaM from the black mulberry (Morus nigra) in complex with mannose.
SourceFEBS J. 272:3725-3732(2005).
PubMed ID16008570
DOI10.1111/j.1742-4658.2005.04801.x

3AuthorsGallego del Sol F. Nagano C. Cavada B.S. Calvete J.J.
TitleThe first crystal structure of a Mimosoideae lectin reveals a novel quaternary arrangement of a widespread domain.
SourceJ. Mol. Biol. 353:574-583(2005).
PubMed ID16185708
DOI10.1016/j.jmb.2005.08.055

4AuthorsKanagawa M. Satoh T. Ikeda A. Nakano Y. Yagi H. Kato K. Kojima-Aikawa K. Yamaguchi Y.
TitleCrystal structures of human secretory proteins ZG16p and ZG16b reveal a Jacalin-related beta-prism fold.
SourceBiochem. Biophys. Res. Commun. 404:201-205(2011).
PubMed ID21110947
DOI10.1016/j.bbrc.2010.11.093

5AuthorsChang W.-C. Liu K.-L. Hsu F.-C. Jeng S.-T. Cheng Y.-S.
TitleIpomoelin, a jacalin-related lectin with a compact tetrameric association and versatile carbohydrate binding properties regulated by its N terminus.
SourcePLoS ONE 7:E40618-E40618(2012).
PubMed ID22808208
DOI10.1371/journal.pone.0040618



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