2z48

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{{STRUCTURE_2z48| PDB=2z48 | SCENE= }}
{{STRUCTURE_2z48| PDB=2z48 | SCENE= }}
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'''Crystal Structure of Hemolytic Lectin CEL-III Complexed with GalNac'''
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===Crystal Structure of Hemolytic Lectin CEL-III Complexed with GalNac===
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==Overview==
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CEL-III is a Ca(2+)-dependent hemolytic lectin, isolated from the marine invertebrate Cucumaria echinata. The three-dimensional structure of CEL-III/GalNAc and CEL-III/methyl alpha-galactoside complexes was solved by x-ray crystallographic analysis. In these complexes, five carbohydrate molecules were found to be bound to two carbohydrate-binding domains (domains 1 and 2) located in the N-terminal 2/3 portion of the polypeptide and that contained beta-trefoil folds similar to ricin B-chain. The 3-OH and 4-OH of bound carbohydrate molecules were coordinated with Ca(2+) located at the subdomains 1alpha, 1gamma, 2alpha, 2beta, and 2gamma, simultaneously forming hydrogen bond networks with nearby amino acid side chains, which is similar to carbohydrate binding in C-type lectins. The binding of carbohydrates was further stabilized by aromatic amino acid residues, such as tyrosine and tryptophan, through a stacking interaction with the hydrophobic face of carbohydrates. The importance of amino acid residues in the carbohydrate-binding sites was confirmed by the mutational analyses. The orientation of bound GalNAc and methyl alpha-galactoside was similar to the galactose moiety of lactose bound to the carbohydrate-binding site of the ricin B-chain, although the ricin B-chain does not require Ca(2+) ions for carbohydrate binding. The binding of the carbohydrates induced local structural changes in carbohydrate-binding sites in subdomains 2alpha and 2beta. Binding of GalNAc also induced a slight change in the main chain structure of domain 3, which could be related to the conformational change upon binding of specific carbohydrates to induce oligomerization of the protein.
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(as it appears on PubMed at http://www.pubmed.gov), where 17977832 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17977832}}
==About this Structure==
==About this Structure==
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[[Category: Pore-forming]]
[[Category: Pore-forming]]
[[Category: Toxin]]
[[Category: Toxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 19:56:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:48:20 2008''

Revision as of 05:48, 28 July 2008

Image:2z48.png

Template:STRUCTURE 2z48

Crystal Structure of Hemolytic Lectin CEL-III Complexed with GalNac

Template:ABSTRACT PUBMED 17977832

About this Structure

2Z48 is a Single protein structure of sequence from Cucumaria echinata. Full crystallographic information is available from OCA.

Reference

C-type lectin-like carbohydrate recognition of the hemolytic lectin CEL-III containing ricin-type -trefoil folds., Hatakeyama T, Unno H, Kouzuma Y, Uchida T, Eto S, Hidemura H, Kato N, Yonekura M, Kusunoki M, J Biol Chem. 2007 Dec 28;282(52):37826-35. Epub 2007 Oct 31. PMID:17977832

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