2bex
From Proteopedia
(Difference between revisions)
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- | [[ | + | ==CRYSTAL STRUCTURE OF PLACENTAL RIBONUCLEASE INHIBITOR IN COMPLEX WITH HUMAN EOSINOPHIL DERIVED NEUROTOXIN AT 2A RESOLUTION== |
+ | <StructureSection load='2bex' size='340' side='right' caption='[[2bex]], [[Resolution|resolution]] 1.99Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2bex]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BEX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BEX FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAK:ALPHA-KETOMALONIC+ACID'>MAK</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a4y|1a4y]], [[1gqv|1gqv]], [[1hi2|1hi2]], [[1hi3|1hi3]], [[1hi4|1hi4]], [[1hi5|1hi5]], [[1k2a|1k2a]]</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] </span></td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bex OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bex RCSB], [http://www.ebi.ac.uk/pdbsum/2bex PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | == 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/be/2bex_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Placental ribonuclease inhibitor (RI) binds diverse mammalian RNases with dissociation constants that are in the femtomolar range. Previous studies on the complexes of RI with RNase A and angiogenin revealed that RI utilises largely distinctive interactions to achieve high affinity for these two ligands. Here we report a 2.0 angstroms resolution crystal structure of RI in complex with a third ligand, eosinophil-derived neurotoxin (EDN), and a mutational analysis based on this structure. The RI-EDN interface is more extensive than those of the other two complexes and contains a considerably larger set of interactions. Few of the contacts present in the RI-angiogenin complex are replicated; the correspondence to the RI-RNase A complex is somewhat greater, but still modest. The energetic contributions of various interface regions differ strikingly from those in the earlier complexes. These findings provide insight into the structural basis for the unusual combination of high avidity and relaxed stringency that RI displays. | ||
- | + | Molecular recognition of human eosinophil-derived neurotoxin (RNase 2) by placental ribonuclease inhibitor.,Iyer S, Holloway DE, Kumar K, Shapiro R, Acharya KR J Mol Biol. 2005 Apr 1;347(3):637-55. PMID:15755456<ref>PMID:15755456</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Ribonuclease|Ribonuclease]] | *[[Ribonuclease|Ribonuclease]] | ||
*[[Ribonuclease inhibitor|Ribonuclease inhibitor]] | *[[Ribonuclease inhibitor|Ribonuclease inhibitor]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Pancreatic ribonuclease]] | [[Category: Pancreatic ribonuclease]] |
Revision as of 02:24, 29 September 2014
CRYSTAL STRUCTURE OF PLACENTAL RIBONUCLEASE INHIBITOR IN COMPLEX WITH HUMAN EOSINOPHIL DERIVED NEUROTOXIN AT 2A RESOLUTION
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Categories: Homo sapiens | Pancreatic ribonuclease | Acharya, K R. | Holloway, D E. | Iyer, S. | Kumar, K. | Shapiro, R. | Eosinophil derived neurotoxin | Hydrolase-inhibitor complex | Hydrolase/inhibitor | Luecine-rich repeat | Molecular recognition | Protein-protein interaction | Ribonuclease inhibitor | Rnase 2