1wmy
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(New page: 200px<br /><applet load="1wmy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wmy, resolution 2.00Å" /> '''Crystal Structure of...)
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Revision as of 22:10, 24 November 2007
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Crystal Structure of C-type Lectin CEL-I from Cucumaria echinata
Overview
CEL-I is a C-type lectin, purified from the sea cucumber Cucumaria, echinata, that shows a high specificity for N-acetylgalactosamine, (GalNAc). We determined the crystal structures of CEL-I and its complex, with GalNAc at 2.0 and 1.7 A resolution, respectively. CEL-I forms a, disulfide-linked homodimer and contains two intramolecular disulfide, bonds, although it lacks one intramolecular disulfide bond that is widely, conserved among various C-type carbohydrate recognition domains (CRDs)., Although the sequence similarity of CEL-I with other C-type CRDs is low, the overall folding of CEL-I was quite similar to those of other C-type, CRDs. The structure of the complex with GalNAc revealed that the basic, recognition mode of GalNAc was very similar to that for the GalNAc-binding, mutant of the mannose-binding protein. However, the acetamido group of, GalNAc appeared to be recognized more strongly by the combination of, hydrogen bonds to Arg115 and van der Waals interaction with Gln70., Mutational analyses, in which Gln70 and/or Arg115 were replaced by, alanine, confirmed that these residues contributed to GalNAc recognition, in a cooperative manner.
About this Structure
1WMY is a Single protein structure of sequence from Cucumaria echinata with CA and MPD as ligands. Full crystallographic information is available from OCA.
Reference
Characteristic recognition of N-acetylgalactosamine by an invertebrate C-type Lectin, CEL-I, revealed by X-ray crystallographic analysis., Sugawara H, Kusunoki M, Kurisu G, Fujimoto T, Aoyagi H, Hatakeyama T, J Biol Chem. 2004 Oct 22;279(43):45219-25. Epub 2004 Aug 19. PMID:15319425
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