1hww: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1hww |SIZE=350|CAPTION= <scene name='initialview01'>1hww</scene>, resolution 1.87Å | |PDB= 1hww |SIZE=350|CAPTION= <scene name='initialview01'>1hww</scene>, resolution 1.87Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SWA:1S-8AB-OCTAHYDRO-INDOLIZIDINE-1A,2A,8B-TRIOL'>SWA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Mannosyl-oligosaccharide_1,3-1,6-alpha-mannosidase Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.114 3.2.1.114] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannosyl-oligosaccharide_1,3-1,6-alpha-mannosidase Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.114 3.2.1.114] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1hty|1HTY]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hww OCA], [http://www.ebi.ac.uk/pdbsum/1hww PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hww RCSB]</span> | |||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Kuntz, D A.]] | [[Category: Kuntz, D A.]] | ||
[[Category: Rose, D R.]] | [[Category: Rose, D R.]] | ||
[[Category: 2 c-terminal beta barrel]] | [[Category: 2 c-terminal beta barrel]] | ||
[[Category: n-terminal alpha-beta domain]] | [[Category: n-terminal alpha-beta domain]] | ||
[[Category: three helix bundle]] | [[Category: three helix bundle]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:11:26 2008'' | ||
Revision as of 18:11, 30 March 2008
| |||||||||||||
| 1hww, resolution 1.87Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | MRD, NAG, SWA, ZN | ||||||||||||
| Activity: | Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase, with EC number 3.2.1.114 | ||||||||||||
| Related: | 1HTY
| ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
GOLGI ALPHA-MANNOSIDASE II IN COMPLEX WITH SWAINSONINE
Overview
Golgi 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.
About this Structure
1HWW is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 30 21:11:26 2008
