1buw
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | Although numerous reports have documented that the S-nitrosylation of | + | 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== | ==Disease== | ||
| Line 18: | Line 18: | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Arnone, A.]] | [[Category: Arnone, A.]] | ||
| - | [[Category: Chan, N | + | [[Category: Chan, N L.]] |
| - | [[Category: Rogers, P | + | [[Category: Rogers, P H.]] |
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: NO]] | [[Category: NO]] | ||
[[Category: oxygen transport and vasodilation]] | [[Category: oxygen transport and vasodilation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:32 2008'' |
Revision as of 09:59, 21 February 2008
|
CRYSTAL STRUCTURE OF S-NITROSO-NITROSYL HUMAN HEMOGLOBIN A
Contents |
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.
Disease
Known diseases associated with this structure: Erythremias, alpha- OMIM:[141800], Erythremias, beta- OMIM:[141900], Erythrocytosis OMIM:[141850], HPFH, deletion type OMIM:[141900], Heinz body anemia OMIM:[141850], Heinz body anemias, alpha- OMIM:[141800], Heinz body anemias, beta- OMIM:[141900], Hemoglobin H disease OMIM:[141850], Hypochromic microcytic anemia OMIM:[141850], Methemoglobinemias, alpha- OMIM:[141800], Methemoglobinemias, beta- OMIM:[141900], Sickle cell anemia OMIM:[141900], Thalassemia, alpha- OMIM:[141850], Thalassemia-beta, dominant inclusion-body OMIM:[141900], Thalassemias, alpha- OMIM:[141800], Thalassemias, beta- OMIM:[141900]
About this Structure
1BUW is a Protein complex structure of sequences from Homo sapiens with and as ligands. The following page contains interesting information on the relation of 1BUW with [Hemoglobin]. Full crystallographic information is available from 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:9843411
Page seeded by OCA on Thu Feb 21 11:59:32 2008
