Linked Life Data

7986646

Source:http://linkedlifedata.com/resource/pubmed/id/7986646

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-1-12
pubmed:abstractText
Small angle X-ray scattering (SAXS) was applied to the binding of the immunosuppressant drug cyclosporin-A to the protein calmodulin. Guinier analysis of the SAXS profiles yielded a radius of gyration, Rg, of 19.7 +/- 0.3 A for the native protein and 16.9 +/- 0.3 A for the drug/protein complex. Maximum entropy (maxent) methods of data analysis were used to calculate the distance distribution function, p(r). From this analysis, the Rg for the native protein is 20.9 +/- 0.1 A and that for the complex 16.7 +/- 0.1 A. The measured SAXS profiles and the derived p(r) for calmodulin agree with profiles calculated from the crystallographic structure of calmodulin. Major structural changes are induced in calmodulin on binding cyclosporin-A. A model consistent with the observed scattering profiles is an ellipsoid with major axes 55 and 36 A. Molecular modeling of the calmodulin molecule suggests that bond rotation in the flexible alpha-helix linker region produces models consistent with the above observations.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1047-8477
pubmed:author
pubmed:issnType
Print
pubmed:volume
112
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
192-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
A small angle X-ray scattering study of the binding of cyclosporin-A to calmodulin.
pubmed:affiliation
ANP Program, Australian Nuclear Science and Technology Organisation, Menai NSW.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't