Sandbox136: Difference between revisions

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Anum-II is a Lys49 Phospholipase A2 (<scene name='Sandbox136/Lys/1'>K49</scene>PLA2),protein extracted from ''Atropoides nummifer'' (a snake from central america). Lys49PLA2s are widespread in the venom of several vipers and are structurally classified as group II PLA2s, although the molecular mechanism of their myotoxicity remains unknown. K49-PLA2 possess the ability to disrupt biological membrane which lead to a significant muscle-tissue loss and disability in severely envenomed patients.

Anum-II is a Lys49 Phospholipase A2 (<scene name='Sandbox136/Lys/1'>K49</scene>PLA2),protein extracted from [http://en.wikipedia.org/wiki/Atropoides_nummifer ''Atropoides nummifer''] (a snake from central america). Lys49PLA2s are widespread in the venom of several vipers and are structurally classified as group II PLA2s, although the molecular mechanism of their myotoxicity remains unknown. K49-PLA2 possess the ability to disrupt biological membrane which lead to a significant muscle-tissue loss and disability in severely envenomed patients.

== '''Structure''' ==

Anum-II has a length of 134 amino-acids. The phospholipase is formed by a short N-terminalαhelix (between residues 2-12), a 2nd αhelix (residues 40-55), two-stranded antiparallel <scene name='Sandbox136/Feuillets/1'>sheet</scene> linked thanks to a βwing (74-85) and a 3rd αhelix (residues 90-107). The 3rd αhelix is bound to the 2nd αhelix (in an antiparallele way) thanks to <scene name='Sandbox136/Disulfide/1'>disulfide bonds </scene> ([Cys 44-Cys 105] and [Cys 51-Cys 98]) and thus form a <scene name='Sandbox136/Stabilisation/1'>rigid platform</scene>. The protein is stabilized by 5 other disulfides bonds [Cys 27-Cys 125], [Cys 29-Cys 45] [Cys 50 Cys 134] [Cys 61-Cys 91] [Cys84-Cys96]. Alignment of Anum-II with other PLA2 have revealed that the positions of amino-acid residues which form the ~~catalytic~~ apparatus are conserved (His48,Tyr52, Tyr73 and Asp99) except for Asp49 which is replaced by Lys 49.

Anum-II has a length of 134 amino-acids. The phospholipase is formed by a short N-terminalαhelix (between residues 2-12), a 2nd αhelix (residues 40-55), two-stranded antiparallel <scene name='Sandbox136/Feuillets/1'>sheet</scene> linked thanks to a βwing (74-85) and a 3rd αhelix (residues 90-107). The 3rd αhelix is bound to the 2nd αhelix (in an antiparallele way) thanks to <scene name='Sandbox136/Disulfide/1'>disulfide bonds </scene> ([Cys 44-Cys 105] and [Cys 51-Cys 98]) and thus form a <scene name='Sandbox136/Stabilisation/1'>rigid platform</scene>. The protein is stabilized by 5 other disulfides bonds [Cys 27-Cys 125], [Cys 29-Cys 45] [Cys 50 Cys 134] [Cys 61-Cys 91] [Cys84-Cys96]. Alignment of Anum-II with other PLA2 have revealed that the positions of amino-acid residues which form the <scene name='Sandbox136/Site_catalytique/2'>catalityc apparatus</scene> are conserved (His48,Tyr52, Tyr73 and Asp99) except for Asp49 which is replaced by Lys 49.

The structure of the protein has revealed the presence of an anion-binding site (Murakami ''et al.'', 2006) between <scene name='Sandbox136/Anion/2'>R34</scene>, <scene name='Sandbox136/Anion/2'>K53</scene> and a water molecule (see Figure 3). Sulfate ion is anchored thanks to hydrogen bonds between:

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-Anum-II is a Lys49 Phospholipase A2 (<scene name='Sandbox136/Lys/1'>K49</scene>PLA2),protein extracted from ''Atropoides nummifer'' (a snake from central america). Lys49PLA2s are widespread in the venom of several vipers and are structurally classified as group II PLA2s, although the molecular mechanism of their myotoxicity remains unknown.  K49-PLA2 possess the ability to disrupt biological membrane which lead to a significant muscle-tissue loss and disability in severely envenomed patients.
+Anum-II is a Lys49 Phospholipase A2 (<scene name='Sandbox136/Lys/1'>K49</scene>PLA2),protein extracted from [http://en.wikipedia.org/wiki/Atropoides_nummifer ''Atropoides nummifer''] (a snake from central america). Lys49PLA2s are widespread in the venom of several vipers and are structurally classified as group II PLA2s, although the molecular mechanism of their myotoxicity remains unknown.  K49-PLA2 possess the ability to disrupt biological membrane which lead to a significant muscle-tissue loss and disability in severely envenomed patients.
 == '''Structure''' ==
-Anum-II has a length of 134 amino-acids. The phospholipase is formed by a short N-terminalαhelix (between residues 2-12), a 2nd αhelix (residues 40-55), two-stranded antiparallel <scene name='Sandbox136/Feuillets/1'>sheet</scene> linked thanks to a βwing (74-85) and a 3rd αhelix (residues 90-107). The 3rd αhelix is bound to the 2nd αhelix (in an antiparallele way) thanks to <scene name='Sandbox136/Disulfide/1'>disulfide bonds </scene> ([Cys 44-Cys 105] and [Cys 51-Cys 98]) and thus form a <scene name='Sandbox136/Stabilisation/1'>rigid platform</scene>. The protein is stabilized by 5 other disulfides bonds [Cys 27-Cys 125], [Cys 29-Cys 45] [Cys 50 Cys 134] [Cys 61-Cys 91] [Cys84-Cys96]. Alignment of Anum-II with other PLA2 have revealed that the positions of amino-acid residues which form the catalytic apparatus are conserved (His48,Tyr52, Tyr73 and Asp99) except for Asp49 which is replaced by Lys 49.
+Anum-II has a length of 134 amino-acids. The phospholipase is formed by a short N-terminalαhelix (between residues 2-12), a 2nd αhelix (residues 40-55), two-stranded antiparallel <scene name='Sandbox136/Feuillets/1'>sheet</scene> linked thanks to a βwing (74-85) and a 3rd αhelix (residues 90-107). The 3rd αhelix is bound to the 2nd αhelix (in an antiparallele way) thanks to <scene name='Sandbox136/Disulfide/1'>disulfide bonds </scene> ([Cys 44-Cys 105] and [Cys 51-Cys 98]) and thus form a <scene name='Sandbox136/Stabilisation/1'>rigid platform</scene>. The protein is stabilized by 5 other disulfides bonds [Cys 27-Cys 125], [Cys 29-Cys 45] [Cys 50 Cys 134] [Cys 61-Cys 91] [Cys84-Cys96]. Alignment of Anum-II with other PLA2 have revealed that the positions of amino-acid residues which form the <scene name='Sandbox136/Site_catalytique/2'>catalityc apparatus</scene>  are conserved (His48,Tyr52, Tyr73 and Asp99) except for Asp49 which is replaced by Lys 49.
 The structure of the protein has revealed  the presence of an anion-binding site (Murakami ''et al.'', 2006) between <scene name='Sandbox136/Anion/2'>R34</scene>, <scene name='Sandbox136/Anion/2'>K53</scene>  and a water molecule (see Figure 3). Sulfate ion is anchored thanks to hydrogen bonds between: