1is3: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==LACTOSE AND MES-LIGANDED CONGERIN II== | ==LACTOSE AND MES-LIGANDED CONGERIN II== | ||
<StructureSection load='1is3' size='340' side='right' caption='[[1is3]], [[Resolution|resolution]] 1.45Å' scene=''> | <StructureSection load='1is3' size='340' side='right'caption='[[1is3]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1is3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anguilla_myriaster Anguilla myriaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IS3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IS3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1is3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anguilla_myriaster Anguilla myriaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IS3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IS3 FirstGlance]. <br> | ||
| Line 34: | Line 34: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Anguilla myriaster]] | [[Category: Anguilla myriaster]] | ||
[[Category: Large Structures]] | |||
[[Category: Ishii, C]] | [[Category: Ishii, C]] | ||
[[Category: Kamiya, H]] | [[Category: Kamiya, H]] | ||
Revision as of 13:29, 30 October 2019
LACTOSE AND MES-LIGANDED CONGERIN IILACTOSE AND MES-LIGANDED CONGERIN II
Structural highlights
Function[LEG2_CONMY] This protein binds beta-galactoside. Its physiological function is not yet known. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of congerin II, a galectin family lectin from conger eel, was determined at 1.45A resolution. The previously determined structure of its isoform, congerin I, had revealed a fold evolution via strand swap; however, the structure of congerin II described here resembles other prototype galectins. A comparison of the two congerin genes with that of several other galectins suggests acceralated evolution of both congerin genes following gene duplication. The presence of a Mes (2-[N-morpholino]ethanesulfonic acid) molecule near the carbohydrate-binding site in the crystal structure points to the possibility of an additional binding site in congerin II. The binding site consists of a group of residues that had been replaced following gene duplication suggesting that the binding site was built under selective pressure. Congerin II may be a protein specialized for biological defense with an affinity for target carbohydrates on parasites' cell surface. Crystal structure of a conger eel galectin (congerin II) at 1.45A resolution: implication for the accelerated evolution of a new ligand-binding site following gene duplication.,Shirai T, Matsui Y, Shionyu-Mitsuyama C, Yamane T, Kamiya H, Ishii C, Ogawa T, Muramoto K J Mol Biol. 2002 Aug 30;321(5):879-89. PMID:12206768[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||