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.


1qmo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qmo.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1qmo.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qmo| PDB=1qmo | SCENE= }}
{{STRUCTURE_1qmo| PDB=1qmo | SCENE= }}
-
'''STRUCTURE OF FRIL, A LEGUME LECTIN THAT DELAYS HEMATOPOIETIC PROGENITOR MATURATION'''
+
===STRUCTURE OF FRIL, A LEGUME LECTIN THAT DELAYS HEMATOPOIETIC PROGENITOR MATURATION===
-
==Overview==
+
<!--
-
Binding of multivalent glycoconjugates by lectins often leads to the formation of cross-linked complexes. Type I cross-links, which are one-dimensional, are formed by a divalent lectin and a divalent glycoconjugate. Type II cross-links, which are two or three-dimensional, occur when a lectin or glycoconjugate has a valence greater than two. Type II complexes are a source of additional specificity, since homogeneous type II complexes are formed in the presence of mixtures of lectins and glycoconjugates. This additional specificity is thought to become important when a lectin interacts with clusters of glycoconjugates, e.g. as is present on the cell surface. The cryst1al structure of the Glc/Man binding legume lectin FRIL in complex with a trisaccharide provides a molecular snapshot of how weak protein-protein interactions, which are not observed in solution, can become important when a cross-linked complex is formed. In solution, FRIL is a divalent dimer, but in the crystal FRIL forms a tetramer, which allows for the formation of an intricate type II cross-linked complex with the divalent trisaccharide. The dependence on weak protein-protein interactions can ensure that a specific type II cross-linked complex and its associated specificity can occur only under stringent conditions, which explains why lectins are often found forming higher-order oligomers.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10843844}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10843844 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10843844}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Lectin]]
[[Category: Lectin]]
[[Category: Sugar complex]]
[[Category: Sugar complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:27:29 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:45:55 2008''

Revision as of 17:45, 28 July 2008

Template:STRUCTURE 1qmo

STRUCTURE OF FRIL, A LEGUME LECTIN THAT DELAYS HEMATOPOIETIC PROGENITOR MATURATION

Template:ABSTRACT PUBMED 10843844

About this Structure

1QMO is a Protein complex structure of sequences from Lablab purpureus. Full crystallographic information is available from OCA.

Reference

The role of weak protein-protein interactions in multivalent lectin-carbohydrate binding: crystal structure of cross-linked FRIL., Hamelryck TW, Moore JG, Chrispeels MJ, Loris R, Wyns L, J Mol Biol. 2000 Jun 16;299(4):875-83. PMID:10843844

Page seeded by OCA on Mon Jul 28 20:45:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools