1ae7: Difference between revisions

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==Overview==

The three-dimensional structure of notexin has been solved by molecular, replacement methods. The structure has been refined at 2.0 A resolution to, a crystallographic R-value of 16.5% with good stereo-chemistry. The core, of the protein is very similar to other phospholipase A2s (PLA2 s) but, several parts of the molecule are distinctly different. The most, significant differences from PLA2 s from bovine pancreas and rattlesnake, occur in the stretches 56-80 and 85-89. Residue 69, which has been shown, to be important for phospholipase binding, has a different conformation, and different interactions than in other known PLA2s. The C alpha, positions for residues 86-88 differ by about 6 A from both the bovine and, the rattlesnake enzyme. The crystals contain no Ca2+ ions. Instead, a, water molecule occupies the calcium site.

The three-dimensional structure of notexin has been solved by molecular replacement methods. The structure has been refined at 2.0 A resolution to a crystallographic R-value of 16.5% with good stereo-chemistry. The core of the protein is very similar to other phospholipase A2s (PLA2 s) but several parts of the molecule are distinctly different. The most significant differences from PLA2 s from bovine pancreas and rattlesnake occur in the stretches 56-80 and 85-89. Residue 69, which has been shown to be important for phospholipase binding, has a different conformation and different interactions than in other known PLA2s. The C alpha positions for residues 86-88 differ by about 6 A from both the bovine and the rattlesnake enzyme. The crystals contain no Ca2+ ions. Instead, a water molecule occupies the calcium site.

==About this Structure==

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[[Category: venom]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The three-dimensional structure of notexin has been solved by molecular, replacement methods. The structure has been refined at 2.0 A resolution to, a crystallographic R-value of 16.5% with good stereo-chemistry. The core, of the protein is very similar to other phospholipase A2s (PLA2 s) but, several parts of the molecule are distinctly different. The most, significant differences from PLA2 s from bovine pancreas and rattlesnake, occur in the stretches 56-80 and 85-89. Residue 69, which has been shown, to be important for phospholipase binding, has a different conformation, and different interactions than in other known PLA2s. The C alpha, positions for residues 86-88 differ by about 6 A from both the bovine and, the rattlesnake enzyme. The crystals contain no Ca2+ ions. Instead, a, water molecule occupies the calcium site.
+The three-dimensional structure of notexin has been solved by molecular replacement methods. The structure has been refined at 2.0 A resolution to a crystallographic R-value of 16.5% with good stereo-chemistry. The core of the protein is very similar to other phospholipase A2s (PLA2 s) but several parts of the molecule are distinctly different. The most significant differences from PLA2 s from bovine pancreas and rattlesnake occur in the stretches 56-80 and 85-89. Residue 69, which has been shown to be important for phospholipase binding, has a different conformation and different interactions than in other known PLA2s. The C alpha positions for residues 86-88 differ by about 6 A from both the bovine and the rattlesnake enzyme. The crystals contain no Ca2+ ions. Instead, a water molecule occupies the calcium site.
 ==About this Structure==
@@ Line 26: / Line 26: @@
 [[Category: venom]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:29:51 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:43:31 2008''