3htc: Difference between revisions

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==Overview==

The crystallographic structure of a recombinant hirudin-thrombin complex, has been solved at 2.3 angstrom (A) resolution. Hirudin consists of an, NH2-terminal globular domain and a long (39 A) COOH-terminal extended, domain. Residues Ile1 to Tyr3 of hirudin form a parallel beta-strand with, Ser214 to Glu217 of thrombin with the nitrogen atom of Ile1 making a, hydrogen bond with Ser195 O gamma atom of the catalytic site, but the, specificity pocket of thrombin is not involved in the interaction. The, COOH-terminal segment makes numerous electrostatic interactions with an, anion-binding exosite of thrombin, whereas the last five residues are in a, helical loop that forms many hydrophobic contacts. In all, 27 of the 65, residues of hirudin have contacts less than 4.0 A with thrombin (10 ion, pairs and 23 hydrogen bonds). Such abundant interactions may account for, the high affinity and specificity of hirudin.

The crystallographic structure of a recombinant hirudin-thrombin complex has been solved at 2.3 angstrom (A) resolution. Hirudin consists of an NH2-terminal globular domain and a long (39 A) COOH-terminal extended domain. Residues Ile1 to Tyr3 of hirudin form a parallel beta-strand with Ser214 to Glu217 of thrombin with the nitrogen atom of Ile1 making a hydrogen bond with Ser195 O gamma atom of the catalytic site, but the specificity pocket of thrombin is not involved in the interaction. The COOH-terminal segment makes numerous electrostatic interactions with an anion-binding exosite of thrombin, whereas the last five residues are in a helical loop that forms many hydrophobic contacts. In all, 27 of the 65 residues of hirudin have contacts less than 4.0 A with thrombin (10 ion pairs and 23 hydrogen bonds). Such abundant interactions may account for the high affinity and specificity of hirudin.

==Disease==

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[[Category: Bode, W.]]

[[Category: Huber, R.]]

[[Category: Ravichandran, K.G.]]

[[Category: Ravichandran, K G.]]

[[Category: Rydel, T.J.]]

[[Category: Rydel, T J.]]

[[Category: Tulinsky, A.]]

[[Category: hydrolase(serine protease)]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 17~~:43:28 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:10:07 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The crystallographic structure of a recombinant hirudin-thrombin complex, has been solved at 2.3 angstrom (A) resolution. Hirudin consists of an, NH2-terminal globular domain and a long (39 A) COOH-terminal extended, domain. Residues Ile1 to Tyr3 of hirudin form a parallel beta-strand with, Ser214 to Glu217 of thrombin with the nitrogen atom of Ile1 making a, hydrogen bond with Ser195 O gamma atom of the catalytic site, but the, specificity pocket of thrombin is not involved in the interaction. The, COOH-terminal segment makes numerous electrostatic interactions with an, anion-binding exosite of thrombin, whereas the last five residues are in a, helical loop that forms many hydrophobic contacts. In all, 27 of the 65, residues of hirudin have contacts less than 4.0 A with thrombin (10 ion, pairs and 23 hydrogen bonds). Such abundant interactions may account for, the high affinity and specificity of hirudin.
+The crystallographic structure of a recombinant hirudin-thrombin complex has been solved at 2.3 angstrom (A) resolution. Hirudin consists of an NH2-terminal globular domain and a long (39 A) COOH-terminal extended domain. Residues Ile1 to Tyr3 of hirudin form a parallel beta-strand with Ser214 to Glu217 of thrombin with the nitrogen atom of Ile1 making a hydrogen bond with Ser195 O gamma atom of the catalytic site, but the specificity pocket of thrombin is not involved in the interaction. The COOH-terminal segment makes numerous electrostatic interactions with an anion-binding exosite of thrombin, whereas the last five residues are in a helical loop that forms many hydrophobic contacts. In all, 27 of the 65 residues of hirudin have contacts less than 4.0 A with thrombin (10 ion pairs and 23 hydrogen bonds). Such abundant interactions may account for the high affinity and specificity of hirudin.
 ==Disease==
@@ Line 20: / Line 20: @@
 [[Category: Bode, W.]]
 [[Category: Huber, R.]]
-[[Category: Ravichandran, K.G.]]
+[[Category: Ravichandran, K G.]]
-[[Category: Rydel, T.J.]]
+[[Category: Rydel, T J.]]
 [[Category: Tulinsky, A.]]
 [[Category: hydrolase(serine protease)]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:43:28 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:10:07 2008''