1dwr: Difference between revisions

Revision as of 23:44, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1dwr.png

Template:STRUCTURE 1dwr

MYOGLOBIN (HORSE HEART) WILD-TYPE COMPLEXED WITH COMYOGLOBIN (HORSE HEART) WILD-TYPE COMPLEXED WITH CO

Template:ABSTRACT PUBMED 10706294

About this StructureAbout this Structure

1DWR is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobin., Chu K, Vojtchovsky J, McMahon BH, Sweet RM, Berendzen J, Schlichting I, Nature. 2000 Feb 24;403(6772):921-3. PMID:10706294

Page seeded by OCA on Mon Jun 30 23:44:10 2008

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 {{STRUCTURE_1dwr|  PDB=1dwr  |  SCENE=  }}
-'''MYOGLOBIN (HORSE HEART) WILD-TYPE COMPLEXED WITH CO'''
+===MYOGLOBIN (HORSE HEART) WILD-TYPE COMPLEXED WITH CO===
-==Overview==
+<!--
-Small molecules such as NO, O2, CO or H2 are important biological ligands that bind to metalloproteins to function crucially in processes such as signal transduction, respiration and catalysis. A key issue for understanding the regulation of reaction mechanisms in these systems is whether ligands gain access to the binding sites through specific channels and docking sites, or by random diffusion through the protein matrix. A model system for studying this issue is myoglobin, a simple haem protein. Myoglobin has been studied extensively by spectroscopy, crystallography, computation and theory. It serves as an aid to oxygen diffusion but also binds carbon monoxide, a byproduct of endogenous haem catabolism. Molecular dynamics simulations, random mutagenesis and flash photolysis studies indicate that ligand migration occurs through a limited number of pathways involving docking sites. Here we report the 1.4 A resolution crystal structure of a ligand-binding intermediate in carbonmonoxy myoglobin that may have far-reaching implications for understanding the dynamics of ligand binding and catalysis.
+The line below this paragraph, {{ABSTRACT_PUBMED_10706294}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10706294 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10706294}}
 ==About this Structure==
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 [[Category: Oxygen transport]]
 [[Category: Respiratory protein]]
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