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L-type lectin domain


FieldValue
SymbolLectin_leg-like
NameLectin_leg-like
imagePDB 1r1z EBI.jpg
captionthe crystal structure of the carbohydrate recognition domain of the glycoprotein sorting receptor p58/ergic-53 reveals a novel metal binding site and conformational changes associated with calcium ion binding
PfamPF03388
Pfam_clanCL0004
InterProIPR005052
SCOP1gv9
Membranome family719

In molecular biology the L-like lectin domain is a protein domain found in lectins which are similar to the leguminous plant lectins.

Lectins are structurally diverse proteins that bind to specific carbohydrates. This family includes the VIP36 and ERGIC-53 lectins. Although proteins containing this domain were originally identified as a family of animal lectins, there are also yeast representatives.

ERGIC-53 is a 53kDa protein, localised to the intermediate region between the endoplasmic reticulum and the Golgi apparatus (ER-Golgi-Intermediate Compartment, ERGIC). It was identified as a calcium-dependent, mannose-specific lectin. Its dysfunction has been associated with combined factors V and VIII deficiency, suggesting an important and substrate-specific role for ERGIC-53 in the glycoprotein-secreting pathway.

The L-like lectin domain has an overall globular shape composed of a beta-sandwich of two major twisted antiparallel beta-sheets. The beta-sandwich comprises a major concave beta-sheet and a minor convex beta-sheet, in a variation of the jelly roll fold.

References

References

  1. (June 1994). "A putative novel class of animal lectins in the secretory pathway homologous to leguminous lectins". Cell.
  2. (March 1996). "ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins". Mol. Biol. Cell.
  3. (April 1999). "ERGIC-53 gene structure and mutation analysis in 19 combined factors V and VIII deficiency families". Blood.
  4. (May 2002). "Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum". J. Biol. Chem..
  5. (December 2003). "The crystal structure of the carbohydrate-recognition domain of the glycoprotein sorting receptor p58/ERGIC-53 reveals an unpredicted metal-binding site and conformational changes associated with calcium ion binding". J. Mol. Biol..
  6. (April 2006). "Structures of the carbohydrate recognition domain of Ca2+-independent cargo receptors Emp46p and Emp47p". J. Biol. Chem..
  7. (September 2007). "Structural basis for recognition of high mannose type glycoproteins by mammalian transport lectin VIP36". J. Biol. Chem..
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