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.


1les

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1les.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1les.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1les| PDB=1les | SCENE= }}
{{STRUCTURE_1les| PDB=1les | SCENE= }}
-
'''LENTIL LECTIN COMPLEXED WITH SUCROSE'''
+
===LENTIL LECTIN COMPLEXED WITH SUCROSE===
-
==Overview==
+
<!--
-
The conformational features of sucrose in the combining site of lentil lectin have been characterized through elucidation of a crystalline complex at 1.9-A resolution, transferred nuclear Overhauser effect experiments performed at 600 Mhz, and molecular modeling. In the crystal, the lentil lectin dimer binds one sucrose molecule per monomer. The locations of 229 water molecules have been identified. NMR experiments have provided 11 transferred NOEs. In parallel, the docking study and conformational analysis of sucrose in the combining site of lentil lectin indicate that three different conformations can be accommodated. Of these, the orientation with lowest energy is identical with the one observed in the crystalline complex and provides good agreement with the observed transferred NOEs. These structural investigations indicate that the bound sucrose has a unique conformation for the glycosidic linkage, close to the one observed in crystalline sucrose, whereas the fructofuranose ring remains relatively flexible and does not exhibit any strong interaction with the protein. Major differences in the hydrogen bonding network of sucrose are found. None of the two inter-residue hydrogen bonds in crystalline sucrose are conserved in the complex with the lectin. Instead, a water molecule bridges hydroxyl groups O2-g and O3-f of sucrose.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7592736}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7592736 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7592736}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Loris, R.]]
[[Category: Loris, R.]]
[[Category: Protein-sugar interaction]]
[[Category: Protein-sugar interaction]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:51:17 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:11:28 2008''

Revision as of 03:11, 29 July 2008

Image:1les.png

Template:STRUCTURE 1les

LENTIL LECTIN COMPLEXED WITH SUCROSE

Template:ABSTRACT PUBMED 7592736

About this Structure

1LES is a Protein complex structure of sequences from Lens culinaris. Full crystallographic information is available from OCA.

Reference

NMR, molecular modeling, and crystallographic studies of lentil lectin-sucrose interaction., Casset F, Hamelryck T, Loris R, Brisson JR, Tellier C, Dao-Thi MH, Wyns L, Poortmans F, Perez S, Imberty A, J Biol Chem. 1995 Oct 27;270(43):25619-28. PMID:7592736

Page seeded by OCA on Tue Jul 29 06:11:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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