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5vpm

From Proteopedia

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Crystal Structure of Human Renin in Complex with a biphenylpipderidinylcarbinol

Structural highlights

5vpm is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Gene:	REN (HUMAN)
Activity:	Renin, with EC number 3.4.23.15
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

Discovery 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.

References

↑ Gribouval O, Gonzales M, Neuhaus T, Aziza J, Bieth E, Laurent N, Bouton JM, Feuillet F, Makni S, Ben Amar H, Laube G, Delezoide AL, Bouvier R, Dijoud F, Ollagnon-Roman E, Roume J, Joubert M, Antignac C, Gubler MC. Mutations in genes in the renin-angiotensin system are associated with autosomal recessive renal tubular dysgenesis. Nat Genet. 2005 Sep;37(9):964-8. Epub 2005 Aug 14. PMID:16116425 doi:ng1623
↑ Zivna M, Hulkova H, Matignon M, Hodanova K, Vylet'al P, Kalbacova M, Baresova V, Sikora J, Blazkova H, Zivny J, Ivanek R, Stranecky V, Sovova J, Claes K, Lerut E, Fryns JP, Hart PS, Hart TC, Adams JN, Pawtowski A, Clemessy M, Gasc JM, Gubler MC, Antignac C, Elleder M, Kapp K, Grimbert P, Bleyer AJ, Kmoch S. Dominant renin gene mutations associated with early-onset hyperuricemia, anemia, and chronic kidney failure. Am J Hum Genet. 2009 Aug;85(2):204-13. Epub 2009 Aug 6. PMID:19664745 doi:10.1016/j.ajhg.2009.07.010
↑ 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. Discovery of renin inhibitors containing a simple aspartate binding moiety that imparts reduced P450 inhibition. Bioorg Med Chem Lett. 2017 Sep 23. pii: S0960-894X(17)30954-X. doi:, 10.1016/j.bmcl.2017.09.046. PMID:28985999 doi:http://dx.doi.org/10.1016/j.bmcl.2017.09.046

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5vpm"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Human Renin in Complex with a biphenylpipderidinylcarbinol==
-<StructureSection load='5vpm' size='340' side='right' caption='[[5vpm]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+<StructureSection load='5vpm' size='340' side='right'caption='[[5vpm]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VPM FirstGlance]. <br>
+<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='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=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>
+<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>
 == Disease ==
@@ Line 21: / Line 22: @@
 </div>
 <div class="pdbe-citations 5vpm" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Renin|Renin]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Renin]]
 [[Category: Concha, N]]

5vpm

From Proteopedia

Current revision

Crystal Structure of Human Renin in Complex with a biphenylpipderidinylcarbinol

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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