Linked Life Data

19642109

Source:http://linkedlifedata.com/resource/pubmed/id/19642109

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2009-10-12
pubmed:abstractText
The tumor suppressor p53 interacts with the redox copper protein Azurin (AZ) forming a complex which is of some relevance in biomedicine and cancer therapy. To obtain information on the spatial organization of this complex when it is immobilized on a substrate, we have used tapping mode-atomic force microscopy (TM-AFM) imaging combined with computational docking. The vertical dimension and the bearing volume of the DNA binding domain (DBD) of p53, anchored to functionalized gold substrate through exposed lysine residues, alone and after deposing AZ, have been measured by TM-AFM. By a computational docking approach, a three-dimensional model for the DBD of p53, before and after addition of AZ, have been predicted. Then we have calculated the possible arrangements of these biomolecular systems on gold substrate by finding a good agreement with the related experimental distribution of the height. The potentiality of the approach combining TM-AFM imaging and computational docking for the study of biomolecular complexes immobilized on substrates is briefly discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1099-1352
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
506-15
pubmed:meshHeading
pubmed:articleTitle
A combined atomic force microscopy imaging and docking study to investigate the complex between p53 DNA binding domain and Azurin.
pubmed:affiliation
Biophysics & Nanoscience Centre, CNISM, Facolta' di Scienze, Università della Tuscia, I-01100 Viterbo, Italy. bizzarri@unitus.it
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't