1hww: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1hww.png|left|200px]]
-{{STRUCTURE_1hww|  PDB=1hww  |  SCENE=  }}
+==GOLGI ALPHA-MANNOSIDASE II IN COMPLEX WITH SWAINSONINE==
+<StructureSection load='1hww' size='340' side='right'caption='[[1hww]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1hww]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1HWW FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.87&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hww OCA], [https://pdbe.org/1hww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hww RCSB], [https://www.ebi.ac.uk/pdbsum/1hww PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hww ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MAN2_DROME 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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hw/1hww_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hww ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===GOLGI ALPHA-MANNOSIDASE II IN COMPLEX WITH SWAINSONINE===
+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<ref>PMID:11406577</ref>
-{{ABSTRACT_PUBMED_11406577}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 1hww" style="background-color:#fffaf0;"></div>
-[[1hww]] is a 1 chain structure of [[Mannosidase]] with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HWW OCA].
 ==See Also==
-*[[Mannosidase|Mannosidase]]
+*[[Mannosidase 3D structures|Mannosidase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:011406577</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Drosophila melanogaster]]
-[[Category: Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase]]
+[[Category: Large Structures]]
-[[Category: Elsen, J M.H van den.]]
+[[Category: Kuntz DA]]
-[[Category: Kuntz, D A.]]
+[[Category: Rose DR]]
-[[Category: Rose, D R.]]
+[[Category: Van den Elsen JMH]]
-[[Category: 2 c-terminal beta barrel]]
-[[Category: Hydrolase]]
-[[Category: N-terminal alpha-beta domain]]
-[[Category: Three helix bundle]]