1h0d: Difference between revisions

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[[Image:1h0d.~~gif~~|left|200px]]

[[Image:1h0d.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF HUMAN ANGIOGENIN IN COMPLEX WITH FAB FRAGMENT OF ITS MONOCLONAL ANTIBODY MAB 26-2F~~'''~~

===CRYSTAL STRUCTURE OF HUMAN ANGIOGENIN IN COMPLEX WITH FAB FRAGMENT OF ITS MONOCLONAL ANTIBODY MAB 26-2F===

~~==Overview==~~

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The ~~murine monoclonal antibody 26-2F neutralizes~~ the ~~angiogenic and ribonucleolytic activities of human angiogenin~~ (~~ANG) and is highly effective in preventing the establishment and metastatic dissemination of human tumors in athymic mice~~. ~~Here we report a 2~~.~~0 A resolution crystal structure for the complex of ANG with the Fab fragment of 26-2F that reveals the detailed interactions between ANG and the complementarity-determining regions (CDRs~~) ~~of the antibody. Surprisingly~~, ~~Fab binding induces a dramatic conformational change in the cell binding region of ANG at~~ the ~~opposite end of the molecule from the combining site; crosslinking experiments indicate that this rearrangement also occurs in solution~~. ~~The ANG~~-~~Fab complex structure should be invaluable for designing maximally humanized versions of 26~~-~~2F for potential clinical use.~~

The line below this paragraph, {{ABSTRACT_PUBMED_12842050}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12842050 is the PubMed ID number.

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==About this Structure==

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[[Category: Antibody]]

[[Category: Ribonuclease]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 18~~:15:21 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:24:47 2008''

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-[[Image:1h0d.gif|left|200px]]
+{{Seed}}
+[[Image:1h0d.png|left|200px]]
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 {{STRUCTURE_1h0d|  PDB=1h0d  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF HUMAN ANGIOGENIN IN COMPLEX WITH FAB FRAGMENT OF ITS MONOCLONAL ANTIBODY MAB 26-2F'''
+===CRYSTAL STRUCTURE OF HUMAN ANGIOGENIN IN COMPLEX WITH FAB FRAGMENT OF ITS MONOCLONAL ANTIBODY MAB 26-2F===
-==Overview==
+<!--
-The murine monoclonal antibody 26-2F neutralizes the angiogenic and ribonucleolytic activities of human angiogenin (ANG) and is highly effective in preventing the establishment and metastatic dissemination of human tumors in athymic mice. Here we report a 2.0 A resolution crystal structure for the complex of ANG with the Fab fragment of 26-2F that reveals the detailed interactions between ANG and the complementarity-determining regions (CDRs) of the antibody. Surprisingly, Fab binding induces a dramatic conformational change in the cell binding region of ANG at the opposite end of the molecule from the combining site; crosslinking experiments indicate that this rearrangement also occurs in solution. The ANG-Fab complex structure should be invaluable for designing maximally humanized versions of 26-2F for potential clinical use.
+The line below this paragraph, {{ABSTRACT_PUBMED_12842050}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12842050 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12842050}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Antibody]]
 [[Category: Ribonuclease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:15:21 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 06:24:47 2008''