This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1dgl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1dgl.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1dgl.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1dgl| PDB=1dgl | SCENE= }}
{{STRUCTURE_1dgl| PDB=1dgl | SCENE= }}
-
'''LECTIN FROM DIOCLEA GRANDIFLORA COMPLEXED TO TRIMANNOSIDE'''
+
===LECTIN FROM DIOCLEA GRANDIFLORA COMPLEXED TO TRIMANNOSIDE===
-
==Overview==
+
<!--
-
The seed lectin from Dioclea grandiflora (DGL) has recently been shown to possess high affinity for 3, 6-di-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranose, the core trimannoside of asparagine-linked carbohydrates, but lower affinity for biantennary complex carbohydrates. In the previous paper, the thermodynamics of DGL binding to deoxy analogs of the core trimannoside and to a biantennary complex carbohydrate were determined by isothermal titration microcalorimetry. The data suggest that DGL recognizes specific hydroxyl groups of the trimannoside similar to that of the jack bean lectin concanavalin A (ConA) (Gupta, D. Dam, T. K., Oscarson, S., and Brewer, C. F. (1997) J. Biol. Chem. 272, 6388-6392). However, the thermodynamics of DGL binding to certain deoxy analogs and to the complex carbohydrate are different from that of ConA. In the present paper, the x-ray crystal structure of DGL complexed to the core trimannoside was determined to a resolution of 2.6 A. The overall structure of the DGL complex is similar to the structure of the ConA-trimannoside complex (Naismith, J. H., and Field, R. A. (1996) J. Biol. Chem. 271, 972-976). The location and conformation of the bound trimannoside as well as its hydrogen-bonding interactions in both complexes are nearly identical. However, differences exist in the location of two loops outside of the respective binding sites containing residues 114-125 and 222-227. The latter residues affect the location of a network of hydrogen-bonded water molecules that interact with the trisaccharide. Differences in the arrangement of ordered water molecules in the binding site and/or protein conformational differences outside of the binding site may account for the differences in the thermodynamics of binding of the two lectins to deoxy analogs of the trimannoside. Molecular modeling studies suggest how DGL discriminates against binding the biantennary complex carbohydrate relative to ConA.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9830028}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9830028 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9830028}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Saccharide binding]]
[[Category: Saccharide binding]]
[[Category: Trimannoside]]
[[Category: Trimannoside]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:50:11 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:03:15 2008''

Revision as of 20:03, 30 June 2008

Image:1dgl.png

Template:STRUCTURE 1dgl

LECTIN FROM DIOCLEA GRANDIFLORA COMPLEXED TO TRIMANNOSIDE

Template:ABSTRACT PUBMED 9830028

About this Structure

1DGL is a Single protein structure of sequence from Dioclea grandiflora. Full crystallographic information is available from OCA.

Reference

Crystal structure of the lectin from Dioclea grandiflora complexed with core trimannoside of asparagine-linked carbohydrates., Rozwarski DA, Swami BM, Brewer CF, Sacchettini JC, J Biol Chem. 1998 Dec 4;273(49):32818-25. PMID:9830028

Page seeded by OCA on Mon Jun 30 23:03:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dgl"
Personal tools