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| | <StructureSection load='2bex' size='340' side='right'caption='[[2bex]], [[Resolution|resolution]] 1.99Å' scene=''> | | <StructureSection load='2bex' size='340' side='right'caption='[[2bex]], [[Resolution|resolution]] 1.99Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2bex]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human Human]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2BEX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2bex]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2BEX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAK:ALPHA-KETOMALONIC+ACID'>MAK</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]] 1.99Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a4y|1a4y]], [[1gqv|1gqv]], [[1hi2|1hi2]], [[1hi3|1hi3]], [[1hi4|1hi4]], [[1hi5|1hi5]], [[1k2a|1k2a]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAK:ALPHA-KETOMALONIC+ACID'>MAK</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] </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=2bex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bex OCA], [https://pdbe.org/2bex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bex RCSB], [https://www.ebi.ac.uk/pdbsum/2bex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bex 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=2bex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bex OCA], [https://pdbe.org/2bex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bex RCSB], [https://www.ebi.ac.uk/pdbsum/2bex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bex ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RINI_HUMAN RINI_HUMAN]] Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis.<ref>PMID:14515218</ref> <ref>PMID:12578357</ref> <ref>PMID:17292889</ref>
| + | [https://www.uniprot.org/uniprot/RINI_HUMAN RINI_HUMAN] Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis.<ref>PMID:14515218</ref> <ref>PMID:12578357</ref> <ref>PMID:17292889</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pancreatic ribonuclease]]
| + | [[Category: Acharya KR]] |
| - | [[Category: Acharya, K R]] | + | [[Category: Holloway DE]] |
| - | [[Category: Holloway, D E]] | + | [[Category: Iyer S]] |
| - | [[Category: Iyer, S]] | + | [[Category: Kumar K]] |
| - | [[Category: Kumar, K]] | + | [[Category: Shapiro R]] |
| - | [[Category: Shapiro, R]] | + | |
| - | [[Category: Eosinophil derived neurotoxin]]
| + | |
| - | [[Category: Hydrolase-inhibitor complex]]
| + | |
| - | [[Category: Hydrolase/inhibitor]]
| + | |
| - | [[Category: Luecine-rich repeat]]
| + | |
| - | [[Category: Molecular recognition]]
| + | |
| - | [[Category: Protein-protein interaction]]
| + | |
| - | [[Category: Ribonuclease inhibitor]]
| + | |
| - | [[Category: Rnase 2]]
| + | |
| Structural highlights
Function
RINI_HUMAN Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis.[1] [2] [3]
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
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Huang GH, Yang GZ, Chen JY, Wu XF. [Expression of a human ribonuclease inhibitor variant in Escherichia coli and silkworm insect cell (Bombyx mori)]. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2003 Oct;35(10):960-3. PMID:14515218
- ↑ Teufel DP, Kao RY, Acharya KR, Shapiro R. Mutational analysis of the complex of human RNase inhibitor and human eosinophil-derived neurotoxin (RNase 2). Biochemistry. 2003 Feb 18;42(6):1451-9. PMID:12578357 doi:10.1021/bi026852o
- ↑ Monti DM, Montesano Gesualdi N, Matousek J, Esposito F, D'Alessio G. The cytosolic ribonuclease inhibitor contributes to intracellular redox homeostasis. FEBS Lett. 2007 Mar 6;581(5):930-4. Epub 2007 Feb 6. PMID:17292889 doi:10.1016/j.febslet.2007.01.072
- ↑ Iyer S, Holloway DE, Kumar K, Shapiro R, Acharya KR. Molecular recognition of human eosinophil-derived neurotoxin (RNase 2) by placental ribonuclease inhibitor. J Mol Biol. 2005 Apr 1;347(3):637-55. PMID:15755456 doi:10.1016/j.jmb.2005.01.035
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