1buw

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1buw, resolution 1.9Å

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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 HEM and NO 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

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