In molecular biology, the X8 domain, is thought to play a role in targeting the plasmodesmata by providing it with structural support. The domain is able to do this since it contains signal sequences for a glycosylphosphatidylinositol (GPI) linkage to the extracellular face of the plasma membrane. This domain is involved in carbohydrate binding.[1]
X8 | |||||||||
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Identifiers | |||||||||
Symbol | X8 | ||||||||
Pfam | PF07983 | ||||||||
InterPro | IPR012946 | ||||||||
SCOP2 | 1occ / SCOPe / SUPFAM | ||||||||
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Structure
editThe X8 domain[2] contains 6 conserved cysteine residues that presumably form three disulphide bridges. The domain is also found in an Olive pollen allergen[3] as well as at the C terminus of family 17 glycosyl hydrolases.[4]
References
edit- ^ Simpson C, Thomas C, Findlay K, Bayer E, Maule AJ (2009). "An Arabidopsis GPI-anchor plasmodesmal neck protein with callose binding activity and potential to regulate cell-to-cell trafficking". Plant Cell. 21 (2): 581–94. doi:10.1105/tpc.108.060145. PMC 2660613. PMID 19223515.
- ^ Henrissat B, Davies GJ (December 2000). "Glycoside hydrolases and glycosyltransferases. Families, modules, and implications for genomics". Plant Physiol. 124 (4): 1515–9. doi:10.1104/pp.124.4.1515. PMC 1539306. PMID 11115868.
- ^ Barral P, Batanero E, Palomares O, Quiralte J, Villalba M, RodrÃguez R (March 2004). "A major allergen from pollen defines a novel family of plant proteins and shows intra- and interspecies [correction of interspecie] cross-reactivity". J. Immunol. 172 (6): 3644–51. doi:10.4049/jimmunol.172.6.3644. PMID 15004167.
- ^ Henrissat B, Coutinho PM, Davies GJ (September 2001). "A census of carbohydrate-active enzymes in the genome of Arabidopsis thaliana". Plant Mol. Biol. 47 (1–2): 55–72. doi:10.1007/978-94-010-0668-2_4. ISBN 978-94-010-3861-4. PMID 11554480.