1bim: Difference between revisions
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<StructureSection load='1bim' size='340' side='right' caption='[[1bim]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='1bim' size='340' side='right' caption='[[1bim]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1bim]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1bim]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BIM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BIM FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0QB:(2S)-2-[(2-AMINO-1,3-THIAZOL-4-YL)METHYL]-N~1~-{(1S,2S)-1-(CYCLOHEXYLMETHYL)-2-HYDROXY-2-[(3R)-1,5,5-TRIMETHYL-2-OXOPYRROLIDIN-3-YL]ETHYL}-N~4~-[2-(DIMETHYLAMINO)-2-OXOETHYL]-N~4~-[(1S)-1-PHENYLETHYL]BUTANEDIAMIDE'>0QB</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0QB:(2S)-2-[(2-AMINO-1,3-THIAZOL-4-YL)METHYL]-N~1~-{(1S,2S)-1-(CYCLOHEXYLMETHYL)-2-HYDROXY-2-[(3R)-1,5,5-TRIMETHYL-2-OXOPYRROLIDIN-3-YL]ETHYL}-N~4~-[2-(DIMETHYLAMINO)-2-OXOETHYL]-N~4~-[(1S)-1-PHENYLETHYL]BUTANEDIAMIDE'>0QB</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CMV IE-HUMAN PREPRORENIN CDNA, REN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CMV IE-HUMAN PREPRORENIN CDNA, REN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Renin Renin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.15 3.4.23.15] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Renin Renin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.15 3.4.23.15] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bim OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bim RCSB], [http://www.ebi.ac.uk/pdbsum/1bim PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bim OCA], [http://pdbe.org/1bim PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bim RCSB], [http://www.ebi.ac.uk/pdbsum/1bim PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1bim" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human]] | ||
[[Category: Renin]] | [[Category: Renin]] | ||
[[Category: Tong, L]] | [[Category: Tong, L]] | ||
Revision as of 01:55, 11 September 2015
CRYSTALLOGRAPHIC STUDIES ON THE BINDING MODES OF P2-P3 BUTANEDIAMIDE RENIN INHIBITORSCRYSTALLOGRAPHIC STUDIES ON THE BINDING MODES OF P2-P3 BUTANEDIAMIDE RENIN INHIBITORS
Structural highlights
Disease[RENI_HUMAN] Defects in REN are a cause of renal tubular dysgenesis (RTD) [MIM:267430]. RTD is an autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype).[1] Defects in REN are the cause of familial juvenile hyperuricemic nephropathy type 2 (HNFJ2) [MIM:613092]. It is a renal disease characterized by juvenile onset of hyperuricemia, slowly progressive renal failure and anemia.[2] Function[RENI_HUMAN] Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney. 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 PubMedThe binding modes of three peptidomimetic P2-P3 butanediamide renin inhibitors have been determined by x-ray crystallography. The inhibitors are bound with their backbones in an extended conformation, and their side chains occupying the S5 to S1' pockets. A (2-amino-4-thiazolyl)methyl side chain at the P2 position shows stronger hydrogen-bonding and van der Waals interactions with renin than the His side chain, which is present in the natural substrate. The ACHPA-gamma-lactam transition state analog has similar interactions with renin as the dihydroxyethylene transition state analog. Crystallographic studies on the binding modes of P2-P3 butanediamide renin inhibitors.,Tong L, Pav S, Lamarre D, Simoneau B, Lavallee P, Jung G J Biol Chem. 1995 Dec 8;270(49):29520-4. PMID:7493993[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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