1vip
From Proteopedia
| Line 5: | Line 5: | ||
==Overview== | ==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, ... | + | 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== | ==About this Structure== | ||
| - | 1VIP is a | + | 1VIP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Daboia_russellii_russellii Daboia russellii russellii] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Structure known Active Site: S1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VIP OCA]. |
==Reference== | ==Reference== | ||
| Line 27: | Line 27: | ||
[[Category: phospholipase a2]] | [[Category: phospholipase a2]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:28:53 2007'' |
Revision as of 10:23, 5 November 2007
|
ANTICOAGULANT CLASS II PHOSPHOLIPASE A2 FROM THE VENOM OF VIPERA RUSSELLI RUSSELLI
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.
About this Structure
1VIP is a Single protein structure of sequence from Daboia russellii russellii with SO4 as ligand. Active as Phospholipase A(2), with EC number 3.1.1.4 Structure known Active Site: S1. Full crystallographic information is available from OCA.
Reference
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 Mon Nov 5 12:28:53 2007
