2voi: Difference between revisions

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[[Image:2voi.~~jpg~~|left|200px]]

[[Image:2voi.png|left|200px]]

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~~'''~~STRUCTURE OF MOUSE A1 BOUND TO THE BID BH3-DOMAIN~~'''~~

===STRUCTURE OF MOUSE A1 BOUND TO THE BID BH3-DOMAIN===

~~==Overview==~~

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~~Apoptotic pathways are regulated by protein~~-~~protein interactions. Interaction of the BH3 domains of proapoptotic Bcl~~-~~2 family proteins with the hydrophobic groove of prosurvival proteins is critical. Whereas some BH3 domains bind in a promiscuous manner~~, ~~others exhibit considerable selectivity and the sequence characteristics that distinguish these activities are unclear. In this study~~, ~~crystal structures of complexes between~~ the ~~prosurvival protein A1 and~~ the ~~BH3 domains from Puma, Bmf, Bak, and Bid have been solved. The structure of A1 is similar to that of other prosurvival proteins, although features, such~~ as ~~an acidic patch in the binding groove, may allow specific therapeutic modulation of apoptosis~~. ~~Significant conformational plasticity was observed in the intermolecular interactions and these differences explain some of the variation in affinity~~. ~~This study~~, ~~in combination with published data, suggests that interactions between conserved residues demarcate optimal binding~~.

The line below this paragraph, {{ABSTRACT_PUBMED_18462686}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 18462686 is the PubMed ID number.

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==About this Structure==

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[[Category: Pro-survival]]

[[Category: Protein-protein complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu May 22 22~~:32:47 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:45:09 2008''

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-[[Image:2voi.jpg|left|200px]]
+{{Seed}}
+[[Image:2voi.png|left|200px]]
 <!--
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 {{STRUCTURE_2voi|  PDB=2voi  |  SCENE=  }}
-'''STRUCTURE OF MOUSE A1 BOUND TO THE BID BH3-DOMAIN'''
+===STRUCTURE OF MOUSE A1 BOUND TO THE BID BH3-DOMAIN===
-==Overview==
+<!--
-Apoptotic pathways are regulated by protein-protein interactions. Interaction of the BH3 domains of proapoptotic Bcl-2 family proteins with the hydrophobic groove of prosurvival proteins is critical. Whereas some BH3 domains bind in a promiscuous manner, others exhibit considerable selectivity and the sequence characteristics that distinguish these activities are unclear. In this study, crystal structures of complexes between the prosurvival protein A1 and the BH3 domains from Puma, Bmf, Bak, and Bid have been solved. The structure of A1 is similar to that of other prosurvival proteins, although features, such as an acidic patch in the binding groove, may allow specific therapeutic modulation of apoptosis. Significant conformational plasticity was observed in the intermolecular interactions and these differences explain some of the variation in affinity. This study, in combination with published data, suggests that interactions between conserved residues demarcate optimal binding.
+The line below this paragraph, {{ABSTRACT_PUBMED_18462686}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18462686 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18462686}}
 ==About this Structure==
@@ Line 35: / Line 39: @@
 [[Category: Pro-survival]]
 [[Category: Protein-protein complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 22:32:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:45:09 2008''