1buw: Difference between revisions

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==Overview==

Although numerous reports have documented that the S-nitrosylation of, cysteine residues by NO alters the activities of a wide variety of, proteins, the direct visualization and the structural consequences of this, reversible modification have not yet been reported for any protein. Here, we describe the crystal structure of S-nitroso-nitrosylhemoglobin, determined at a resolution of 1.8 A. The specific reaction of NO with, Cys93beta is confirmed in this structure, and a large, S-nitrosylation-induced change in the tertiary structure of the, COOH-terminal dipeptides of the beta subunits provides additional insight, into the stereochemical mechanism by which blood flow is regulated by the, interaction of NO with hemoglobin.

Although numerous reports have documented that the S-nitrosylation of cysteine residues by NO alters the activities of a wide variety of proteins, the direct visualization and the structural consequences of this reversible modification have not yet been reported for any protein. Here we describe the crystal structure of S-nitroso-nitrosylhemoglobin determined at a resolution of 1.8 A. The specific reaction of NO with Cys93beta is confirmed in this structure, and a large S-nitrosylation-induced change in the tertiary structure of the COOH-terminal dipeptides of the beta subunits provides additional insight into the stereochemical mechanism by which blood flow is regulated by the interaction of NO with hemoglobin.

==Disease==

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[[Category: Protein complex]]

[[Category: Arnone, A.]]

[[Category: Chan, N.L.]]

[[Category: Chan, N L.]]

[[Category: Rogers, P.H.]]

[[Category: Rogers, P H.]]

[[Category: HEM]]

[[Category: NO]]

[[Category: oxygen transport and vasodilation]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 15~~:33:34 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:32 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Although numerous reports have documented that the S-nitrosylation of, cysteine residues by NO alters the activities of a wide variety of, proteins, the direct visualization and the structural consequences of this, reversible modification have not yet been reported for any protein. Here, we describe the crystal structure of S-nitroso-nitrosylhemoglobin, determined at a resolution of 1.8 A. The specific reaction of NO with, Cys93beta is confirmed in this structure, and a large, S-nitrosylation-induced change in the tertiary structure of the, COOH-terminal dipeptides of the beta subunits provides additional insight, into the stereochemical mechanism by which blood flow is regulated by the, interaction of NO with hemoglobin.
+Although numerous reports have documented that the S-nitrosylation of cysteine residues by NO alters the activities of a wide variety of proteins, the direct visualization and the structural consequences of this reversible modification have not yet been reported for any protein. Here we describe the crystal structure of S-nitroso-nitrosylhemoglobin determined at a resolution of 1.8 A. The specific reaction of NO with Cys93beta is confirmed in this structure, and a large S-nitrosylation-induced change in the tertiary structure of the COOH-terminal dipeptides of the beta subunits provides additional insight into the stereochemical mechanism by which blood flow is regulated by the interaction of NO with hemoglobin.
 ==Disease==
@@ Line 18: / Line 18: @@
 [[Category: Protein complex]]
 [[Category: Arnone, A.]]
-[[Category: Chan, N.L.]]
+[[Category: Chan, N L.]]
-[[Category: Rogers, P.H.]]
+[[Category: Rogers, P H.]]
 [[Category: HEM]]
 [[Category: NO]]
 [[Category: oxygen transport and vasodilation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:33:34 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:32 2008''