1bil: Difference between revisions

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~~{{Seed}}~~

~~[[Image:1bil.png|left|200px]]~~

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==CRYSTALLOGRAPHIC STUDIES ON THE BINDING MODES OF P2-P3 BUTANEDIAMIDE RENIN INHIBITORS==

~~The line below this paragraph~~, ~~containing~~ "~~STRUCTURE_1bil~~"~~, creates the~~ "~~Structure Box~~" ~~on the page~~.

~~You may change the PDB parameter~~ (~~which sets~~ the ~~PDB file loaded into~~ the ~~applet~~)

== Structural highlights ==

or the ~~SCENE parameter (which sets~~ the ~~initial scene displayed when~~ the ~~page is loaded)~~,

<table><tr><td colspan='2'>[[1bil]] is a 2 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=1BIL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BIL FirstGlance]. <br>

~~or leave~~ the ~~SCENE parameter empty for~~ the ~~default display~~.

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr>

-->

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0IU:(2S)-2-[(2-AMINO-1,3-THIAZOL-4-YL)METHYL]-N~1~-[(1S,2R,3R)-1-(CYCLOHEXYLMETHYL)-2,3-DIHYDROXY-5-METHYLHEXYL]-N~4~-[2-(DIMETHYLAMINO)-2-OXOETHYL]-N~4~-[(1S)-1-PHENYLETHYL]BUTANEDIAMIDE'>0IU</scene></td></tr>

~~{{STRUCTURE_1bil| PDB~~=~~1bil | SCENE~~= }}

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bil OCA], [https://pdbe.org/1bil PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bil RCSB], [https://www.ebi.ac.uk/pdbsum/1bil PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bil ProSAT]</span></td></tr>

</table>

== Disease ==

[https://www.uniprot.org/uniprot/RENI_HUMAN RENI_HUMAN] Defects in REN are a cause of renal tubular dysgenesis (RTD) [MIM:[https://omim.org/entry/267430 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).<ref>PMID:16116425</ref> Defects in REN are the cause of familial juvenile hyperuricemic nephropathy type 2 (HNFJ2) [MIM:[https://omim.org/entry/613092 613092]. It is a renal disease characterized by juvenile onset of hyperuricemia, slowly progressive renal failure and anemia.<ref>PMID:19664745</ref>

== Function ==

[https://www.uniprot.org/uniprot/RENI_HUMAN 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 ==

[[Image:Consurf_key_small.gif|200px|right]]

Check<jmol>

<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bi/1bil_consurf.spt"</scriptWhenChecked>

<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=1bil ConSurf].

== Publication Abstract from PubMed ==

The 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===~~

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<ref>PMID:7493993</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~<!--~~

==See Also==

~~The line below this paragraph, {{ABSTRACT_PUBMED_7493993}}, adds the Publication Abstract to the page~~

*[[Renin|Renin]]

~~(as it appears on PubMed at http://www.pubmed.gov), where 7493993 is the PubMed ID number.~~

== References ==

~~-->~~

~~{{ABSTRACT_PUBMED_7493993}}~~

__TOC__

</StructureSection>

==~~About this Structure~~==

~~1BIL is a [~~[~~Single protein]] structure of 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=1BIL OCA~~].

==~~Reference~~==

~~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:[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/7493993 7493993]~~

[[Category: Homo sapiens]]

[[Category: ~~Single protein~~]]

[[Category: Large Structures]]

[[Category: Tong, L.]]

[[Category: Tong L]]

~~[[Category: Aspartic proteinase]]~~

~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:13:22 2008''~~

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@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1bil.png|left|200px]]
-<!--
+==CRYSTALLOGRAPHIC STUDIES ON THE BINDING MODES OF P2-P3 BUTANEDIAMIDE RENIN INHIBITORS==
-The line below this paragraph, containing "STRUCTURE_1bil", creates the "Structure Box" on the page.
+<StructureSection load='1bil' size='340' side='right'caption='[[1bil]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1bil]] is a 2 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=1BIL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BIL FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0IU:(2S)-2-[(2-AMINO-1,3-THIAZOL-4-YL)METHYL]-N~1~-[(1S,2R,3R)-1-(CYCLOHEXYLMETHYL)-2,3-DIHYDROXY-5-METHYLHEXYL]-N~4~-[2-(DIMETHYLAMINO)-2-OXOETHYL]-N~4~-[(1S)-1-PHENYLETHYL]BUTANEDIAMIDE'>0IU</scene></td></tr>
-{{STRUCTURE_1bil|  PDB=1bil  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bil OCA], [https://pdbe.org/1bil PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bil RCSB], [https://www.ebi.ac.uk/pdbsum/1bil PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bil ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/RENI_HUMAN RENI_HUMAN] Defects in REN are a cause of renal tubular dysgenesis (RTD) [MIM:[https://omim.org/entry/267430 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).<ref>PMID:16116425</ref>   Defects in REN are the cause of familial juvenile hyperuricemic nephropathy type 2 (HNFJ2) [MIM:[https://omim.org/entry/613092 613092]. It is a renal disease characterized by juvenile onset of hyperuricemia, slowly progressive renal failure and anemia.<ref>PMID:19664745</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/RENI_HUMAN 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 ==
+[[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/bi/1bil_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=1bil ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The 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===
+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<ref>PMID:7493993</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1bil" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_7493993}}, adds the Publication Abstract to the page
+*[[Renin|Renin]]
-(as it appears on PubMed at http://www.pubmed.gov), where 7493993 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_7493993}}
+__TOC__
+</StructureSection>
-==About this Structure==
-BIL is a [[Single protein]] structure of 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=1BIL OCA].
-==Reference==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/7493993 7493993]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Tong, L.]]
+[[Category: Tong L]]
-[[Category: Aspartic proteinase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:13:22 2008''