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| | <StructureSection load='3bpf' size='340' side='right'caption='[[3bpf]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='3bpf' size='340' side='right'caption='[[3bpf]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3bpf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BPF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3BPF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3bpf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BPF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BPF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yvb|1yvb]], [[2ghu|2ghu]], [[1aim|1aim]], [[3bpm|3bpm]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=3bpf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bpf OCA], [http://pdbe.org/3bpf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bpf RCSB], [http://www.ebi.ac.uk/pdbsum/3bpf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bpf ProSAT]</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=3bpf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bpf OCA], [https://pdbe.org/3bpf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bpf RCSB], [https://www.ebi.ac.uk/pdbsum/3bpf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bpf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9N6S8_PLAFA Q9N6S8_PLAFA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Plasmodium falciparum]] | | [[Category: Plasmodium falciparum]] |
| - | [[Category: Brinen, L S]] | + | [[Category: Brinen LS]] |
| - | [[Category: Lee, J H]] | + | [[Category: Lee JH]] |
| - | [[Category: Kerr, I D]] | + | [[Category: Kerr ID]] |
| - | [[Category: Cysteine protease]]
| + | |
| - | [[Category: Falcipain]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Malaria]]
| + | |
| - | [[Category: Thiol protease]]
| + | |
| Structural highlights
Function
Q9N6S8_PLAFA
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 PubMed
Falcipain-2 and falcipain-3 are critical hemoglobinases of Plasmodium falciparum, the most virulent human malaria parasite. We have determined the 2.9 A crystal structure of falcipain-2 in complex with the epoxysuccinate E64 and the 2.5 A crystal structure of falcipain-3 in complex with the aldehyde leupeptin. These complexes represent the first crystal structures of plasmodial cysteine proteases with small molecule inhibitors and the first reported crystal structure of falcipain-3. Our structural analyses indicate that the relative shape and flexibility of the S2 pocket are affected by a number of discrete amino acid substitutions. The cumulative effect of subtle differences, including those at "gatekeeper" positions, may explain the observed kinetic differences between these two closely related enzymes.
Structures of falcipain-2 and falcipain-3 bound to small molecule inhibitors: implications for substrate specificity.,Kerr ID, Lee JH, Pandey KC, Harrison A, Sajid M, Rosenthal PJ, Brinen LS J Med Chem. 2009 Feb 12;52(3):852-7. PMID:19128015[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kerr ID, Lee JH, Pandey KC, Harrison A, Sajid M, Rosenthal PJ, Brinen LS. Structures of falcipain-2 and falcipain-3 bound to small molecule inhibitors: implications for substrate specificity. J Med Chem. 2009 Feb 12;52(3):852-7. PMID:19128015 doi:10.1021/jm8013663
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