Biology:Jacalin-like lectin domain

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Jacalin-like lectin domain
PDB 1c3n EBI.jpg
crystal structure of helianthus tuberosus lectin complexed to man(1-2)man
Identifiers
SymbolJacalin
PfamPF01419
InterProIPR001229
SCOP21jac / SCOPe / SUPFAM

In molecular biology, the jacalin-like lectin domain is a mannose-binding lectin domain with a beta-prism fold consisting of three 4-stranded beta-sheets, with an internal pseudo 3-fold symmetry. Some lectins in this group stimulate distinct T- and B-cell functions, such as Jacalin, which binds to the T-antigen and acts as an agglutinin. This domain is found in 1 to 6 copies in lectins. The domain is also found in the salt-stress induced protein from rice and an animal prostatic spermine-binding protein.

Database of jacalin like lectins and structure function relations.[1] Proteins containing this domain include:

References

  1. Raval et al, "A database analysis of jacalin-like lectins: sequence–structure–function relationships" Glycobiology vol. 14 no. 12 pp. 1247–1263, 2004 http://glycob.oxfordjournals.org/content/14/12/1247.full.pdf
  2. "Crystal structure of the jacalin-T-antigen complex and a comparative study of lectin-T-antigen complexes". J. Mol. Biol. 321 (4): 637–45. August 2002. doi:10.1016/S0022-2836(02)00674-5. PMID 12206779. 
  3. "Structural basis for the carbohydrate specificities of artocarpin: variation in the length of a loop as a strategy for generating ligand specificity". J. Mol. Biol. 338 (4): 757–70. May 2004. doi:10.1016/j.jmb.2004.03.040. PMID 15099743. 
  4. "Structure of the complex of Maclura pomifera agglutinin and the T-antigen disaccharide, Galbeta1,3GalNAc". J. Biol. Chem. 273 (11): 6312–8. March 1998. doi:10.1074/jbc.273.11.6312. PMID 9497359. 
  5. "Helianthus tuberosus lectin reveals a widespread scaffold for mannose-binding lectins". Structure 7 (12): 1473–82. December 1999. doi:10.1016/s0969-2126(00)88338-0. PMID 10647178. 
  6. "The crystal structure of the Calystegia sepium agglutinin reveals a novel quaternary arrangement of lectin subunits with a beta-prism fold". J. Biol. Chem. 279 (1): 527–33. January 2004. doi:10.1074/jbc.M308218200. PMID 14561768. 
  7. "Domain-swapped structure of the potent antiviral protein griffithsin and its mode of carbohydrate binding". Structure 14 (7): 1127–35. July 2006. doi:10.1016/j.str.2006.05.017. PMID 16843894. 
This article incorporates text from the public domain Pfam and InterPro: IPR001229