DNA recognition and structural specificities.

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dc.contributor.authorRoy, K Ben_US
dc.date.accessioned1996-04-01en_US
dc.date.accessioned2009-05-27T09:46:20Z
dc.date.available1996-04-01en_US
dc.date.available2009-05-27T09:46:20Z
dc.date.issued1996-04-01en_US
dc.description26 references.en_US
dc.description.abstractHow a short DNA sequence interacts in a sequence specific manner with appropriate protein is understood only in certain systems for which high resolution crystal structures of the protein-DNA complexes are available. The base sequence of DNA is sensed directly (read-out) by the protein through the major or minor groove, while DNA shape also is sensed through multiple interactions with the sugar phosphate backbone. Several repressors, activators and restriction endonucleases complexed with their cognate DNA oligomers are now known and reviewed here. If the binding site on DNA has two fold symmetry, the protein interacts as dimer and uses a variety of structural motifs for specific interaction. The level of specificity of interaction is enhanced by flexibility and/or distortion in either the DNA or protein tertiary structure.en_US
dc.description.affiliationCentre for Biotechnology, Jawaharlal Nehru University, New Delhi, India.en_US
dc.identifier.citationRoy KB. DNA recognition and structural specificities. Indian Journal of Biochemistry & Biophysics. 1996 Apr; 33(2): 83-7en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/28513
dc.language.isoengen_US
dc.source.urihttps://https://www.niscair.res.in/ScienceCommunication/ResearchJournals/rejour/ijbb/ijbb0.aspen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshDNA-Binding Proteins --chemistryen_US
dc.subject.meshHelix-Loop-Helix Motifsen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshProtein Structure, Secondaryen_US
dc.titleDNA recognition and structural specificities.en_US
dc.typeJournal Articleen_US
dc.typeReviewen_US
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