1pc9: Difference between revisions

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[[Image:1pc9.~~gif~~|left|200px]]

[[Image:1pc9.png|left|200px]]

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~~'''~~Crystal Structure of BnSP-6, a Lys49-Phospholipase A2~~'''~~

===Crystal Structure of BnSP-6, a Lys49-Phospholipase A2===

~~==Overview==~~

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Phospholipases A(2) are components of Bothrops venoms responsible for disruption of cell membrane integrity via hydrolysis of its phospholipids. A class of PLA(2)-like proteins has been described which despite PLA(2) activity on artificial substrate, ~~due to a D49K mutation~~, ~~is still highly myonecrotic. This work reports~~ the ~~X-ray structure determination of two Lys49-PLA(2)s from Bothrops neuwiedi pauloensis (BnSP-7 and BnSP-6) and, for~~ the ~~first time, the comparison of eight dimeric Lys49-PLA~~(~~2)s~~. ~~This comparison reveals that there are not just two ("open" and "closed") but at least six different conformations~~. ~~The binding of fatty acid observed in three recent Lys49-PLA(2~~) ~~structures seems to be independent of their quaternary conformation~~. ~~Cys29 polarization by Lys122 is not significant for BnSP~~-~~7 and BnSP~~-~~6 or other structures not bound by fatty acids. These structures may be in an "active" state when nothing is bound to them and the Lys122/Cys29 interactions are weak or absent.~~

The line below this paragraph, {{ABSTRACT_PUBMED_14623331}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 14623331 is the PubMed ID number.

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==About this Structure==

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[[Category: Myotoxin]]

[[Category: Venom.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 04~~:55:53 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:29:10 2008''

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-[[Image:1pc9.gif|left|200px]]
+{{Seed}}
+[[Image:1pc9.png|left|200px]]
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 {{STRUCTURE_1pc9|  PDB=1pc9  |  SCENE=  }}
-'''Crystal Structure of BnSP-6, a Lys49-Phospholipase A2'''
+===Crystal Structure of BnSP-6, a Lys49-Phospholipase A2===
-==Overview==
+<!--
-Phospholipases A(2) are components of Bothrops venoms responsible for disruption of cell membrane integrity via hydrolysis of its phospholipids. A class of PLA(2)-like proteins has been described which despite PLA(2) activity on artificial substrate, due to a D49K mutation, is still highly myonecrotic. This work reports the X-ray structure determination of two Lys49-PLA(2)s from Bothrops neuwiedi pauloensis (BnSP-7 and BnSP-6) and, for the first time, the comparison of eight dimeric Lys49-PLA(2)s. This comparison reveals that there are not just two ("open" and "closed") but at least six different conformations. The binding of fatty acid observed in three recent Lys49-PLA(2) structures seems to be independent of their quaternary conformation. Cys29 polarization by Lys122 is not significant for BnSP-7 and BnSP-6 or other structures not bound by fatty acids. These structures may be in an "active" state when nothing is bound to them and the Lys122/Cys29 interactions are weak or absent.
+The line below this paragraph, {{ABSTRACT_PUBMED_14623331}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14623331 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14623331}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Myotoxin]]
 [[Category: Venom.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:55:53 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:29:10 2008''