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New page: left|200px<br /> <applet load="1e21" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e21, resolution 1.9Å" /> '''RIBONUCLEASE 1 DES1-... |
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== | ==Ribonuclease 1 des1-7 Crystal Structure at 1.9A== | ||
Human pancreatic ribonuclease 1 (RNase 1) is considered to be the human | <StructureSection load='1e21' size='340' side='right'caption='[[1e21]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1e21]] is a 1 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=1E21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E21 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e21 OCA], [https://pdbe.org/1e21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e21 RCSB], [https://www.ebi.ac.uk/pdbsum/1e21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e21 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RNAS1_HUMAN RNAS1_HUMAN] Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.<ref>PMID:17350650</ref> | |||
== 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/e2/1e21_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=1e21 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Human pancreatic ribonuclease 1 (RNase 1) is considered to be the human counterpart of bovine pancreatic RNase A. Truncation of seven amino-acid residues from the amino-terminal sequence resulted in RNase 1 Delta N7, which has a reduced ribonucleolytic activity and a lower affinity for the human placental RNase inhibitor (PRI). This RNase 1 variant has been cloned, heterologously overexpressed, purified and crystallized. Its crystal structure has been determined and refined using data to 1.9 A resolution. The molecule displays the alpha + beta folding topology typical of members of the RNase A superfamily. The main distinct features found in RNase 1 Delta N7 are basically located in three loops affecting the fitting of the enzyme to the active site of subtilisin and the shape of the B2 subsite. These changes, taken with the lack of the catalytically active residue Lys7, may explain the reduced affinity of RNase 1 Delta N7 for PRI and the low ribonucleolytic activity of the protein when compared with the native enzyme. | |||
Three-dimensional structure of human RNase 1 delta N7 at 1.9 A resolution.,Pous J, Mallorqui-Fernandez G, Peracaula R, Terzyan SS, Futami J, Tada H, Yamada H, Seno M, de Llorens R, Gomis-Ruth FX, Coll M Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):498-505. PMID:11264578<ref>PMID:11264578</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1e21" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Coll M]] | ||
[[Category: | [[Category: De Llorens R]] | ||
[[Category: Futami | [[Category: Futami J]] | ||
[[Category: Gomis-Ruth | [[Category: Gomis-Ruth FX]] | ||
[[Category: Mallorqui-Fernandez G]] | |||
[[Category: Mallorqui-Fernandez | [[Category: Peracaula R]] | ||
[[Category: Peracaula | [[Category: Pous J]] | ||
[[Category: Pous | [[Category: Seno M]] | ||
[[Category: Seno | [[Category: Tada H]] | ||
[[Category: Tada | [[Category: Terzyan SS]] | ||
[[Category: Terzyan | [[Category: Yamada H]] | ||
[[Category: Yamada | |||
Latest revision as of 11:24, 6 November 2024
Ribonuclease 1 des1-7 Crystal Structure at 1.9ARibonuclease 1 des1-7 Crystal Structure at 1.9A
Structural highlights
FunctionRNAS1_HUMAN Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.[1] 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 PubMedHuman pancreatic ribonuclease 1 (RNase 1) is considered to be the human counterpart of bovine pancreatic RNase A. Truncation of seven amino-acid residues from the amino-terminal sequence resulted in RNase 1 Delta N7, which has a reduced ribonucleolytic activity and a lower affinity for the human placental RNase inhibitor (PRI). This RNase 1 variant has been cloned, heterologously overexpressed, purified and crystallized. Its crystal structure has been determined and refined using data to 1.9 A resolution. The molecule displays the alpha + beta folding topology typical of members of the RNase A superfamily. The main distinct features found in RNase 1 Delta N7 are basically located in three loops affecting the fitting of the enzyme to the active site of subtilisin and the shape of the B2 subsite. These changes, taken with the lack of the catalytically active residue Lys7, may explain the reduced affinity of RNase 1 Delta N7 for PRI and the low ribonucleolytic activity of the protein when compared with the native enzyme. Three-dimensional structure of human RNase 1 delta N7 at 1.9 A resolution.,Pous J, Mallorqui-Fernandez G, Peracaula R, Terzyan SS, Futami J, Tada H, Yamada H, Seno M, de Llorens R, Gomis-Ruth FX, Coll M Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):498-505. PMID:11264578[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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