1agi: Difference between revisions

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[[Image:1agi.~~gif~~|left|200px]]

[[Image:1agi.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF BOVINE ANGIOGENIN AT 1.5 ANGSTROMS RESOLUTION~~'''~~

===CRYSTAL STRUCTURE OF BOVINE ANGIOGENIN AT 1.5 ANGSTROMS RESOLUTION===

~~==Overview==~~

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The ~~capacity of angiogenin~~ (~~Ang) to induce blood vessel growth is critically dependent~~ on ~~its ribonucleolytic activity~~. Crystallography and mutagenesis of human Ang have previously shown that its pyrimidine binding site is obstructed by Gln-117, implying that a conformational change is a key part of the mechanism of Ang action. ~~The 1.5-A-resolution crystal structure of bovine Ang~~, ~~in which glutamic acid~~ is ~~substituted for Gln-117, now confirms that a blocked active site is characteristic of these proteins. Indeed,~~ the ~~inactive conformation of bovine Ang is stabilized by a more extensive set of interactions than is that of human Ang~~. ~~The three-dimensional structure of the putative receptor binding site is also well conserved in the two proteins. The Arg~~-~~Gly~~-~~Asp segment of this site in bovine Ang, which is replaced by Arg-Glu-Asn in human Ang, does not have a conformation typical of an integrin recognition site.~~

The line below this paragraph, {{ABSTRACT_PUBMED_7708754}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 7708754 is the PubMed ID number.

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==About this Structure==

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[[Category: Vallee, B L.]]

[[Category: Endonuclease]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 10~~:14:20 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:48:05 2008''

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-[[Image:1agi.gif|left|200px]]
+{{Seed}}
+[[Image:1agi.png|left|200px]]
 <!--
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 {{STRUCTURE_1agi|  PDB=1agi  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF BOVINE ANGIOGENIN AT 1.5 ANGSTROMS RESOLUTION'''
+===CRYSTAL STRUCTURE OF BOVINE ANGIOGENIN AT 1.5 ANGSTROMS RESOLUTION===
-==Overview==
+<!--
-The capacity of angiogenin (Ang) to induce blood vessel growth is critically dependent on its ribonucleolytic activity. Crystallography and mutagenesis of human Ang have previously shown that its pyrimidine binding site is obstructed by Gln-117, implying that a conformational change is a key part of the mechanism of Ang action. The 1.5-A-resolution crystal structure of bovine Ang, in which glutamic acid is substituted for Gln-117, now confirms that a blocked active site is characteristic of these proteins. Indeed, the inactive conformation of bovine Ang is stabilized by a more extensive set of interactions than is that of human Ang. The three-dimensional structure of the putative receptor binding site is also well conserved in the two proteins. The Arg-Gly-Asp segment of this site in bovine Ang, which is replaced by Arg-Glu-Asn in human Ang, does not have a conformation typical of an integrin recognition site.
+The line below this paragraph, {{ABSTRACT_PUBMED_7708754}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7708754 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7708754}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Vallee, B L.]]
 [[Category: Endonuclease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:14:20 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:48:05 2008''