2r0h: Difference between revisions

From Proteopedia
Jump to navigationJump to search
Newer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
New page: left|200px <!-- The line below this paragraph, containing "STRUCTURE_2r0h", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:2r0h.jpg|left|200px]]
{{Seed}}
[[Image:2r0h.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2r0h|  PDB=2r0h  |  SCENE=  }}  
{{STRUCTURE_2r0h|  PDB=2r0h  |  SCENE=  }}  


'''Fungal lectin CGL3 in complex with chitotriose (chitotetraose)'''
===Fungal lectin CGL3 in complex with chitotriose (chitotetraose)===




==Overview==
<!--
Recent advances in genome sequencing efforts have revealed an abundance of novel putative lectins. Among these, many galectin-related proteins, characterized by many conserved residues but intriguingly lacking critical amino acids, have been found in all corners of the eukaryotic superkingdom. Here we present a structural and biochemical analysis of one representative, the galectin-related lectin CGL3 found in the inky cap mushroom Coprinopsis cinerea. This protein contains all but one conserved residues known to be involved in beta-galactoside binding in galectins. A Trp residue strictly conserved among galectins is changed to an Arg in CGL3 (R81). Accordingly, the galectin-related protein is not able to bind lactose. Screening of a glycan array revealed that CGL3 displays preference for oligomers of beta1-4-linked N-acetyl-glucosamines (chitooligosaccharides) and GalNAc beta 1-4GlcNAc (LacdiNAc). Carbohydrate-binding affinity of this novel lectin was quantified using isothermal titration calorimetry, and its mode of chitooligosaccharide coordination not involving any aromatic amino acid residues was studied by X-ray crystallography. Structural information was used to alter the carbohydrate-binding specificity and substrate affinity of CGL3. The importance of residue R81 in determining the carbohydrate-binding specificity was demonstrated by replacing this Arg with a Trp residue (R81W). This single-amino-acid change led to a lectin that failed to bind chitooligosaccharides but gained lactose binding. Our results demonstrate that, similar to the legume lectin fold, the galectin fold represents a conserved structural framework upon which dramatically altered specificities can be grafted by few alterations in the binding site and that, in consequence, many metazoan galectin-related proteins may represent lectins with novel carbohydrate-binding specificities.
The line below this paragraph, {{ABSTRACT_PUBMED_18440554}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 18440554 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_18440554}}


==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Lectin]]
[[Category: Lectin]]
[[Category: Sugar binding protein]]
[[Category: Sugar binding protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 21:37:12 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:13:04 2008''

Revision as of 20:13, 28 July 2008

File:2r0h.png

Template:STRUCTURE 2r0h

Fungal lectin CGL3 in complex with chitotriose (chitotetraose)

Template:ABSTRACT PUBMED 18440554

About this Structure

2R0H is a Single protein structure of sequence from Coprinopsis cinerea. Full crystallographic information is available from OCA.

Reference

Structural basis for chitotetraose coordination by CGL3, a novel galectin-related protein from Coprinopsis cinerea., Walti MA, Walser PJ, Thore S, Grunler A, Bednar M, Kunzler M, Aebi M, J Mol Biol. 2008 May 23;379(1):146-59. Epub 2008 Apr 3. PMID:18440554

Page seeded by OCA on Mon Jul 28 23:13:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2r0h&oldid=718162"