5vpm: Difference between revisions
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==Crystal Structure of Human Renin in Complex with a biphenylpipderidinylcarbinol== | ==Crystal Structure of Human Renin in Complex with a biphenylpipderidinylcarbinol== | ||
<StructureSection load='5vpm' size='340' side='right' caption='[[5vpm]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='5vpm' size='340' side='right'caption='[[5vpm]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5vpm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VPM OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5vpm]] 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=5VPM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5VPM FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9G7:methyl+[(4S)-4-(3-ethyl-6-fluoro[1,1-biphenyl]-2-yl)-4-hydroxy-4-{(3R)-1-[(piperidin-4-yl)acetyl]piperidin-3-yl}butyl]carbamate'>9G7</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9G7:methyl+[(4S)-4-(3-ethyl-6-fluoro[1,1-biphenyl]-2-yl)-4-hydroxy-4-{(3R)-1-[(piperidin-4-yl)acetyl]piperidin-3-yl}butyl]carbamate'>9G7</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">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:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5vpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vpm OCA], [http://pdbe.org/5vpm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vpm RCSB], [http://www.ebi.ac.uk/pdbsum/5vpm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vpm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5vpm" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5vpm" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Renin|Renin]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Large Structures]] | |||
[[Category: Renin]] | [[Category: Renin]] | ||
[[Category: Concha, N]] | [[Category: Concha, N]] | ||
Revision as of 11:42, 30 September 2020
Crystal Structure of Human Renin in Complex with a biphenylpipderidinylcarbinolCrystal Structure of Human Renin in Complex with a biphenylpipderidinylcarbinol
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. Publication Abstract from PubMedDiscovery of potent renin inhibitors which contain a simplified alkylamino Asp-binding group and exhibit improved selectivity for renin over Cyp3A4 is described. Structure-function results in this series are rationalized based on analysis of selected compounds bound to renin, and the contribution of each molecular feature leading to the reduced P450 inhibition is quantified. Discovery of renin inhibitors containing a simple aspartate binding moiety that imparts reduced P450 inhibition.,Lawhorn BG, Tran T, Hong VS, Morgan LA, Le BT, Harpel MR, Jolivette L, Diaz E, Schwartz B, Gross JW, Tomaszek T, Semus S, Concha N, Smallwood A, Holt DA, Kallander LS Bioorg Med Chem Lett. 2017 Sep 23. pii: S0960-894X(17)30954-X. doi:, 10.1016/j.bmcl.2017.09.046. PMID:28985999[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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