Linked Life Data

8636974

Source:http://linkedlifedata.com/resource/pubmed/id/8636974

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1996-7-5
pubmed:abstractText
The structures of deoxy (alpha(Mg(II))2 beta(Fe(II))2) and CO-liganded (alpha(Mg(II)2(Fe(II)-CO)2) forms of human hemoglobin were determined by X-ray crystallography to a resolution of 1.7 A and 1.9 A, respectively. The deoxy hybrid has virtually the same structure as that of the native deoxy HbA. Both the deoxy and CO-liganded hybrids assumed a T quaternary structure characteristic of native deoxy HbA. No significant structural difference was found between the alpha subunits of the CO-liganded hybrid and deoxy HbA, while in the beta subunit, significant tertiary structural changes were confined to the heme pocket. Baldwin showed by a comparison of COHbA and deoxy HbA that there is a 1.5 A shift of the beta subunit heme into its pocket. This shift was much reduced in alpha(Mg(II))2 beta(Fe(II)-CO)2. On the other hand, when the two structures are compared with superposition of hemes, the nearest neighbors of CO (Fe, E11 Val and E7 His) have shifted nearly to the same positions as those in COHbA. Thus the tertiary structure of the beta subunit of alpha(Mg(II))2 beta(Fe(II)-CO)2 is such that the CO molecule and the neighboring atoms assume nearly the same conformation as those of COHbA, while the block shift of these groups is impeded with respect to the structural invariant portions of the molecule.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
255
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
726-34
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
High-resolution crystal structure of magnesium (MgII)-iron (FeII) hybrid hemoglobin with liganded beta subunits.
pubmed:affiliation
Department of Biophysical Engineering, Faculty of Engineering Science, Osaka University, Japan.
pubmed:publicationType
Journal Article, Comparative Study