1wmy
From Proteopedia
(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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| - | [[Image:1wmy.gif|left|200px]]<br /><applet load="1wmy" size=" | + | [[Image:1wmy.gif|left|200px]]<br /><applet load="1wmy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wmy, resolution 2.00Å" /> | caption="1wmy, resolution 2.00Å" /> | ||
'''Crystal Structure of C-type Lectin CEL-I from Cucumaria echinata'''<br /> | '''Crystal Structure of C-type Lectin CEL-I from Cucumaria echinata'''<br /> | ||
==Overview== | ==Overview== | ||
| - | CEL-I is a C-type lectin, purified from the sea cucumber Cucumaria | + | 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== | ==About this Structure== | ||
| - | 1WMY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cucumaria_echinata Cucumaria echinata] with CA and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1WMY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cucumaria_echinata Cucumaria echinata] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WMY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: n-acetylgalactosamine]] | [[Category: n-acetylgalactosamine]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:04 2008'' |
Revision as of 13:46, 21 February 2008
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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 and 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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