1buw: Difference between revisions

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[[Image:1buw.~~jpg~~|left|200px]]

[[Image:1buw.png|left|200px]]

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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.

==About this Structure==

1BUW is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1BUW with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb41_1.html Hemoglobin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BUW OCA].

~~==Reference==~~

Crystal structure of the S-nitroso form of liganded human hemoglobin., Chan NL, Rogers PH, Arnone A, Biochemistry. 1998 Nov 24;37(47):16459-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9843411 9843411]

[[Category: Hemoglobin]]

[[Category: Homo sapiens]]

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[[Category: Rogers, P H.]]

[[Category: Oxygen transport and vasodilation]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 11~~:58:59 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:06:07 2008''

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-[[Image:1buw.jpg|left|200px]]
+[[Image:1buw.png|left|200px]]
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-==Overview==
+{{ABSTRACT_9843411}}
-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.
 ==About this Structure==
 BUW is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1BUW with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb41_1.html Hemoglobin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BUW OCA].
-==Reference==
-Crystal structure of the S-nitroso form of liganded human hemoglobin., Chan NL, Rogers PH, Arnone A, Biochemistry. 1998 Nov 24;37(47):16459-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9843411 9843411]
 [[Category: Hemoglobin]]
 [[Category: Homo sapiens]]
@@ Line 27: / Line 23: @@
 [[Category: Rogers, P H.]]
 [[Category: Oxygen transport and vasodilation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:58:59 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:06:07 2008''