1e21: Difference between revisions

Revision as of 13:22, 21 February 2008

RIBONUCLEASE 1 DES1-7 CRYSTAL STRUCTURE AT 1.9A

OverviewOverview

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.

About this StructureAbout this Structure

1E21 is a Single protein structure of sequence from Homo sapiens. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 12:22:55 2008

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OCA

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-[[Image:1e21.gif|left|200px]]<br />
+[[Image:1e21.gif|left|200px]]<br /><applet load="1e21" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1e21" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1e21, resolution 1.9&Aring;" />
 '''RIBONUCLEASE 1 DES1-7 CRYSTAL STRUCTURE AT 1.9A'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-E21 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E21 OCA].
+E21 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E21 OCA].
 ==Reference==
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 [[Category: Coll, M.]]
 [[Category: Futami, J.]]
-[[Category: Gomis-Ruth, F.X.]]
+[[Category: Gomis-Ruth, F X.]]
-[[Category: Llorens, R.De.]]
+[[Category: Llorens, R De.]]
 [[Category: Mallorqui-Fernandez, G.]]
 [[Category: Peracaula, R.]]
@@ Line 24: / Line 23: @@
 [[Category: Seno, M.]]
 [[Category: Tada, H.]]
-[[Category: Terzyan, S.S.]]
+[[Category: Terzyan, S S.]]
 [[Category: Yamada, H.]]
 [[Category: human pancreatic ribonuclease]]
@@ Line 30: / Line 29: @@
 [[Category: rnase 1]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:38:46 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:55 2008''