3dyh: Difference between revisions

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 <StructureSection load='3dyh' size='340' side='right'caption='[[3dyh]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3dyh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Trypanosoma_(trypanozoon)_brucei Trypanosoma (trypanozoon) brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DYH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3DYH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3dyh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DYH FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=721:3-BUTOXY-1-(2,2-DIPHOSPHONOETHYL)PYRIDINIUM'>721</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ewg|2ewg]], [[2i19|2i19]], [[2ogd|2ogd]], [[3dyf|3dyf]], [[3dyg|3dyg]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=721:3-BUTOXY-1-(2,2-DIPHOSPHONOETHYL)PYRIDINIUM'>721</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/(2E,6E)-farnesyl_diphosphate_synthase (2E,6E)-farnesyl diphosphate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.10 2.5.1.10] </span></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=3dyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dyh OCA], [https://pdbe.org/3dyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dyh RCSB], [https://www.ebi.ac.uk/pdbsum/3dyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dyh ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3dyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dyh OCA], [http://pdbe.org/3dyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dyh RCSB], [http://www.ebi.ac.uk/pdbsum/3dyh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3dyh ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q86C09_9TRYP Q86C09_9TRYP]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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=3dyh ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Considerable effort has focused on the development of selective protein farnesyl transferase (FTase) and protein geranylgeranyl transferase (GGTase) inhibitors as cancer chemotherapeutics. Here, we report a new strategy for anticancer therapeutic agents involving inhibition of farnesyl diphosphate synthase (FPPS) and geranylgeranyl diphosphate synthase (GGPPS), the two enzymes upstream of FTase and GGTase, by lipophilic bisphosphonates. Due to dual site targeting and decreased polarity, the compounds have activities far greater than do current bisphosphonate drugs in inhibiting tumor cell growth and invasiveness, both in vitro and in vivo. We explore how these compounds inhibit cell growth and how cell activity can be predicted based on enzyme inhibition data, and using X-ray diffraction, solid state NMR, and isothermal titration calorimetry, we show how these compounds bind to FPPS and/or GGPPS.
-Lipophilic bisphosphonates as dual farnesyl/geranylgeranyl diphosphate synthase inhibitors: an X-ray and NMR investigation.,Zhang Y, Cao R, Yin F, Hudock MP, Guo RT, Krysiak K, Mukherjee S, Gao YG, Robinson H, Song Y, No JH, Bergan K, Leon A, Cass L, Goddard A, Chang TK, Lin FY, Van Beek E, Papapoulos S, Wang AH, Kubo T, Ochi M, Mukkamala D, Oldfield E J Am Chem Soc. 2009 Apr 15;131(14):5153-62. PMID:19309137<ref>PMID:19309137</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3dyh" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Farnesyl diphosphate synthase 3D structures|Farnesyl diphosphate synthase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Cao, R]]
+[[Category: Trypanosoma brucei]]
-[[Category: Gao, Y]]
+[[Category: Cao R]]
-[[Category: Goddard, A]]
+[[Category: Gao Y]]
-[[Category: Oldfield, E]]
+[[Category: Goddard A]]
-[[Category: Robinson, H]]
+[[Category: Oldfield E]]
-[[Category: Isoprene biosynthesis]]
+[[Category: Robinson H]]
-[[Category: Protein-bisphosphonate complex]]
-[[Category: Transferase]]