1hww: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==GOLGI ALPHA-MANNOSIDASE II IN COMPLEX WITH SWAINSONINE== | ==GOLGI ALPHA-MANNOSIDASE II IN COMPLEX WITH SWAINSONINE== | ||
<StructureSection load='1hww' size='340' side='right' caption='[[1hww]], [[Resolution|resolution]] 1.87Å' scene=''> | <StructureSection load='1hww' size='340' side='right'caption='[[1hww]], [[Resolution|resolution]] 1.87Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1hww]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HWW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HWW FirstGlance]. <br> | <table><tr><td colspan='2'>[[1hww]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HWW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HWW FirstGlance]. <br> | ||
| Line 32: | Line 32: | ||
==See Also== | ==See Also== | ||
*[[Mannosidase|Mannosidase]] | *[[Mannosidase 3D structures|Mannosidase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 38: | Line 38: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Drome]] | [[Category: Drome]] | ||
[[Category: Large Structures]] | |||
[[Category: Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase]] | [[Category: Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase]] | ||
[[Category: Elsen, J M.H van den]] | [[Category: Elsen, J M.H van den]] | ||
Revision as of 13:08, 8 January 2020
GOLGI ALPHA-MANNOSIDASE II IN COMPLEX WITH SWAINSONINEGOLGI ALPHA-MANNOSIDASE II IN COMPLEX WITH SWAINSONINE
Structural highlights
Function[MAN2_DROME] Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway (By similarity). 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 PubMedGolgi alpha-mannosidase II, a key enzyme in N-glycan processing, is a target in the development of anti- cancer therapies. The crystal structure of Drosophila Golgi alpha-mannosidase II in the absence and presence of the anti-cancer agent swainsonine and the inhibitor deoxymannojirimycin reveals a novel protein fold with an active site zinc intricately involved both in the substrate specificity of the enzyme and directly in the catalytic mechanism. Identification of a putative GlcNAc binding pocket in the vicinity of the active site cavity provides a model for the binding of the GlcNAcMan(5)GlcNAc(2) substrate and the consecutive hydrolysis of the alpha1,6- and alpha1,3-linked mannose residues. The enzyme-inhibitor interactions observed provide insight into the catalytic mechanism, opening the door to the design of novel inhibitors of alpha-mannosidase II. Structure of Golgi alpha-mannosidase II: a target for inhibition of growth and metastasis of cancer cells.,van den Elsen JM, Kuntz DA, Rose DR EMBO J. 2001 Jun 15;20(12):3008-17. PMID:11406577[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||