2not: Difference between revisions

Revision as of 19:09, 21 February 2008

NOTECHIS II-5, NEUROTOXIC PHOSPHOLIPASE A2 FROM NOTECHIS SCUTATUS SCUTATUS

OverviewOverview

The three-dimensional structures of the class II anticoagulant phospholipase A2 (PLA2) toxin RVV-VD from the venom of Russell's viper, Vipera russelli russelli, and the class I neurotoxic PLA2 Notechis II-5 from the, Australian tiger snake, Notechis scutatus scutatus, were determined to 2.2 A and 3.0 A resolution, respectively. Both enzymes are monomeric and consist of 121 and 119 residues, respectively. A comparison of ten class I/II PLA2 structures showed, among other differences, that the beta-sheet of these enzymes (residues 76-83) is about 90 degrees less twisted in class I than in class II PLA2s. This, along with the insertion of some residues in the region 57-59 in class I enzymes (the elapid loop), could be the main reason for the significant difference in the anticoagulant and (presynaptic) neurotoxic properties between the two classes of PLA2. It seems apparent from sequence and structural comparisons that the toxic site of PLA2 responsible for the strong anticoagulancy of these toxins consists of a negatively charged part, Glu53, together with a positively charged ridge of lysine residues free for intermolecular interactions. These lysines differ between the two classes of PLA2.

About this StructureAbout this Structure

2NOT is a Single protein structure of sequence from Notechis scutatus scutatus. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.

ReferenceReference

The three-dimensional structures of two toxins from snake venom throw light on the anticoagulant and neurotoxic sites of phospholipase A2., Carredano E, Westerlund B, Persson B, Saarinen M, Ramaswamy S, Eaker D, Eklund H, Toxicon. 1998 Jan;36(1):75-92. PMID:9604284

Page seeded by OCA on Thu Feb 21 18:09:11 2008

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OCA

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-[[Image:2not.gif|left|200px]]<br /><applet load="2not" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2not.gif|left|200px]]<br /><applet load="2not" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2not, resolution 3.0&Aring;" />
 '''NOTECHIS II-5, NEUROTOXIC PHOSPHOLIPASE A2 FROM NOTECHIS SCUTATUS SCUTATUS'''<br />
 ==Overview==
-The three-dimensional structures of the class II anticoagulant, phospholipase A2 (PLA2) toxin RVV-VD from the venom of Russell's viper, Vipera russelli russelli, and the class I neurotoxic PLA2 Notechis II-5, from the, Australian tiger snake, Notechis scutatus scutatus, were, determined to 2.2 A and 3.0 A resolution, respectively. Both enzymes are, monomeric and consist of 121 and 119 residues, respectively. A comparison, of ten class I/II PLA2 structures showed, among other differences, that, the beta-sheet of these enzymes (residues 76-83) is about 90 degrees less, twisted in class I than in class II PLA2s. This, along with the insertion, of some residues in the region 57-59 in class I enzymes (the elapid loop), could be the main reason for the significant difference in the, anticoagulant and (presynaptic) neurotoxic properties between the two, classes of PLA2. It seems apparent from sequence and structural, comparisons that the toxic site of PLA2 responsible for the strong, anticoagulancy of these toxins consists of a negatively charged part, Glu53, together with a positively charged ridge of lysine residues free, for intermolecular interactions. These lysines differ between the two, classes of PLA2.
+The three-dimensional structures of the class II anticoagulant phospholipase A2 (PLA2) toxin RVV-VD from the venom of Russell's viper, Vipera russelli russelli, and the class I neurotoxic PLA2 Notechis II-5 from the, Australian tiger snake, Notechis scutatus scutatus, were determined to 2.2 A and 3.0 A resolution, respectively. Both enzymes are monomeric and consist of 121 and 119 residues, respectively. A comparison of ten class I/II PLA2 structures showed, among other differences, that the beta-sheet of these enzymes (residues 76-83) is about 90 degrees less twisted in class I than in class II PLA2s. This, along with the insertion of some residues in the region 57-59 in class I enzymes (the elapid loop), could be the main reason for the significant difference in the anticoagulant and (presynaptic) neurotoxic properties between the two classes of PLA2. It seems apparent from sequence and structural comparisons that the toxic site of PLA2 responsible for the strong anticoagulancy of these toxins consists of a negatively charged part, Glu53, together with a positively charged ridge of lysine residues free for intermolecular interactions. These lysines differ between the two classes of PLA2.
 ==About this Structure==
-NOT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Notechis_scutatus_scutatus Notechis scutatus scutatus]. Active as [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NOT OCA].
+NOT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Notechis_scutatus_scutatus Notechis scutatus scutatus]. Active as [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NOT OCA].
 ==Reference==
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 [[Category: venom]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:49:14 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:09:11 2008''