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1smr

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(New page: 200px<br /><applet load="1smr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1smr, resolution 2.0&Aring;" /> '''THE 3-D STRUCTURE OF ...)
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[[Image:1smr.gif|left|200px]]<br /><applet load="1smr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1smr, resolution 2.0&Aring;" />
 
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'''THE 3-D STRUCTURE OF MOUSE SUBMAXILLARY RENIN COMPLEXED WITH A DECAPEPTIDE INHIBITOR CH-66 BASED ON THE 4-16 FRAGMENT OF RAT ANGIOTENSINOGEN'''<br />
 
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==Overview==
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==The 3-d structure of mouse submaxillary renin complexed with a decapeptide inhibitor ch-66 based on the 4-16 fragment of rat angiotensinogen==
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The structure of mouse submaxillary renin complexed with a decapeptide, inhibitor, CH-66 (Piv-His-Pro-Phe-His-Leu-OH-Leu-Tyr-Tyr-Ser-NH2), where, Piv denotes a pivaloyl blocking group, and -OH- denotes a hydroxyethylene, (-(S)CHOH-CH2-) transition state isostere as a scissile bond surrogate, has been refined to an agreement factor of 0.18 at 2.0 A resolution. The, positions of 10,038 protein atoms and 364 inhibitor atoms (4 independent, protein inhibitor complexes), as well as of 613 solvent atoms, have been, determined with an estimated root-mean-square (r.m.s.) error of 0.21 A., The r.m.s. deviation from ideality for bond distances is 0.026 A, and for, angle distances is 0.0543 A. We have compared the three-dimensional, structure of mouse renin with other aspartic proteinases, using rigid-body, analysis with respect to shifts involving the domain comprising residues, 190 to 302. In terms of the relative orientation of domains, mouse, submaxillary renin is closest to human renin with only a 1.7 degrees, difference in domain orientation. Porcine pepsin (the molecular, replacement model) differs structurally from mouse renin by a 6.9 degrees, domain rotation, whereas endothiapepsin, a fungal aspartic proteinase, differs by 18.8 degrees. The triple proline loop (residues 292 to 294), which is structurally opposite the active-site "flap" (residues 72 to 83), gives renin a superficial resemblance to the fold of the retroviral, proteinases. The inhibitor is bound in an extended conformation along the, active-site cleft, and the hydroxyethylene moiety forms hydrogen bonds, with both catalytic aspartate carboxylates. The complex is stabilized by, hydrogen bonds between the main chain of the inhibitor and the enzyme. All, side-chains of the inhibitor are in van der Waals contact with groups in, the enzyme and define ten specificity sub-sites. This study shows how, renin has compact sub-sites due to the positioning of secondary structure, elements, to complementary substitutions and to the residue composition of, its loops close to the active site, leading to extreme specificity towards, its prohormone substrate, angiotensinogen. We have analysed the, micro-environment of each of the buried charged groups in order to predict, their ionization states.
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<StructureSection load='1smr' size='340' side='right'caption='[[1smr]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1smr]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SMR FirstGlance]. <br>
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</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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LPL:LEU-HYDROXYETHYLENE-LEU'>LPL</scene>, <scene name='pdbligand=PIV:PIVALIC+ACID'>PIV</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1smr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1smr OCA], [https://pdbe.org/1smr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1smr RCSB], [https://www.ebi.ac.uk/pdbsum/1smr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1smr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RENI2_MOUSE RENI2_MOUSE] Renin is a highly specific endopeptidase, related to pepsin, 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. Its function in the salivary gland is not understood.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sm/1smr_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1smr ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1SMR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SMR OCA].
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*[[Renin|Renin]]
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__TOC__
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==Reference==
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</StructureSection>
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X-ray analysis at 2.0 A resolution of mouse submaxillary renin complexed with a decapeptide inhibitor CH-66, based on the 4-16 fragment of rat angiotensinogen., Dealwis CG, Frazao C, Badasso M, Cooper JB, Tickle IJ, Driessen H, Blundell TL, Murakami K, Miyazaki H, Sueiras-Diaz J, et al., J Mol Biol. 1994 Feb 11;236(1):342-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8107115 8107115]
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Renin]]
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[[Category: Blundell TL]]
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[[Category: Single protein]]
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[[Category: Dealwis CG]]
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[[Category: Blundell, T.L.]]
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[[Category: Dealwis, C.G.]]
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[[Category: hydrolase(aspartic proteinase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:29:48 2007''
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Current revision

The 3-d structure of mouse submaxillary renin complexed with a decapeptide inhibitor ch-66 based on the 4-16 fragment of rat angiotensinogen

PDB ID 1smr

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