Sandbox136: Difference between revisions

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Lys49 PLA2 has a strong ~~myotoxicitic~~ effect. The replacement of Asp49 by <scene name='Sandbox136/Lys_49/1'>Lys49</scene> provides a ~~particular role of~~ the protein. Indeed, Asp49 allows the binding of Ca2+ an essential co-factor which is responsible for the activation of the catalytically apparatus (thanks to conserved amino-acids:His48, Tyr52, Tyr73 and Asp99). Lys49 PLA2 is not able to bind the co-factor, and thus is catalytically inactive. But some recent studies have shown that the Lys49 PLA2 is able to bind to the KDR (receptor of the VEGF165 growth factor)and this corresponds to his myotoxic activity.

Anum-II (Lys49 PLA2) has a strong myotoxic effect. The replacement of Asp49 by <scene name='Sandbox136/Lys_49/1'>Lys49</scene> provides a different activity for the protein. Indeed, Asp49 allows the binding of Ca2+ an essential co-factor which is responsible for the activation of the catalytically apparatus (thanks to conserved amino-acids:His48, Tyr52, Tyr73 and Asp99). Lys49 PLA2 is not able to bind the co-factor, and thus is catalytically inactive. But some recent studies have shown that the Lys49 PLA2 is able to bind to the KDR (receptor of the VEGF165 growth factor)and this corresponds to his myotoxic activity.

Vascular endothelial growth factor (VEGF165) and its ~~receptor~~ Kinase insert domain containing receptor (KDR) are used in mechanisms of regulations of blood vessel formations. Experiments have revealed that the venom extracted from Agkistrodon piscivorus contains a KDR binding protein.It has been shown that this KDRb-p was in fact a Lys49 PLA2.Lys49 is able to bind to the extracellular domain of KDR receptors with a sub-nanomolar affinity. Recently studies revealed the fact that the region of the protein involved in the fixation on KDR was located in the C-terminal region. C- terminal region ~~differ~~ from the rest of the protein in his amino acid sequence, indeed some amino-acids are positive (K,R) and seem to play a role in the recognition and fixation on KDR.

Vascular endothelial growth factor (VEGF165) and its Kinase insert domain containing receptor (KDR) are used in mechanisms of regulations of blood vessel formations. Experiments have revealed that the venom extracted from ''Agkistrodon piscivorus'' contains a KDR binding protein.It has been shown that this KDRb-p was in fact a Lys49 PLA2.Lys49 is able to bind to the extracellular domain of KDR receptors with a sub-nanomolar affinity. Recently studies revealed the fact that the region of the protein involved in the fixation on KDR was located in the C-terminal region. C- terminal region differs from the rest of the protein in his amino acid sequence, indeed some amino-acids are positive (K,R) and seem to play a role in the recognition and fixation on KDR.

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Revision as of 15:50, 14 November 2009 view source Elie Peillon (talk \| contribs) 21 edits →''' Method of Determination''' ← Older edit		Revision as of 15:58, 14 November 2009 view source Elie Peillon (talk \| contribs) 21 edits →'''Physiological effect''' Newer edit →
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	Lys49 PLA2 has a strong ~~myotoxicitic~~ effect. The replacement of Asp49 by <scene name='Sandbox136/Lys_49/1'>Lys49</scene> provides a ~~particular role of~~ the protein. Indeed, Asp49 allows the binding of Ca2+ an essential co-factor which is responsible for the activation of the catalytically apparatus (thanks to conserved amino-acids:His48, Tyr52, Tyr73 and Asp99). Lys49 PLA2 is not able to bind the co-factor, and thus is catalytically inactive. But some recent studies have shown that the Lys49 PLA2 is able to bind to the KDR (receptor of the VEGF165 growth factor)and this corresponds to his myotoxic activity.		Anum-II (Lys49 PLA2) has a strong myotoxic effect. The replacement of Asp49 by <scene name='Sandbox136/Lys_49/1'>Lys49</scene> provides a different activity for the protein. Indeed, Asp49 allows the binding of Ca2+ an essential co-factor which is responsible for the activation of the catalytically apparatus (thanks to conserved amino-acids:His48, Tyr52, Tyr73 and Asp99). Lys49 PLA2 is not able to bind the co-factor, and thus is catalytically inactive. But some recent studies have shown that the Lys49 PLA2 is able to bind to the KDR (receptor of the VEGF165 growth factor)and this corresponds to his myotoxic activity.

	Vascular endothelial growth factor (VEGF165) and its ~~receptor~~ Kinase insert domain containing receptor (KDR) are used in mechanisms of regulations of blood vessel formations. Experiments have revealed that the venom extracted from Agkistrodon piscivorus contains a KDR binding protein.It has been shown that this KDRb-p was in fact a Lys49 PLA2.Lys49 is able to bind to the extracellular domain of KDR receptors with a sub-nanomolar affinity. Recently studies revealed the fact that the region of the protein involved in the fixation on KDR was located in the C-terminal region. C- terminal region ~~differ~~ from the rest of the protein in his amino acid sequence, indeed some amino-acids are positive (K,R) and seem to play a role in the recognition and fixation on KDR.		Vascular endothelial growth factor (VEGF165) and its Kinase insert domain containing receptor (KDR) are used in mechanisms of regulations of blood vessel formations. Experiments have revealed that the venom extracted from ''Agkistrodon piscivorus'' contains a KDR binding protein.It has been shown that this KDRb-p was in fact a Lys49 PLA2.Lys49 is able to bind to the extracellular domain of KDR receptors with a sub-nanomolar affinity. Recently studies revealed the fact that the region of the protein involved in the fixation on KDR was located in the C-terminal region. C- terminal region differs from the rest of the protein in his amino acid sequence, indeed some amino-acids are positive (K,R) and seem to play a role in the recognition and fixation on KDR.