2.50
Hdl Handle:
http://hdl.handle.net/10547/294682
Title:
Role of aromatic amino acids in protein-nucleic acid recognition
Authors:
Baker, Christopher M.; Grant, Guy H.
Abstract:
Statistical analysis of structures from the PBD has been used to examine the role that the aromatic amino acids play in protein-nucleic acid recognition. In protein-DNA complexes, the residues Phe and His are found to bind selectively to the DNA chain--Phe to A and T, and His to T and G. The preferred binding modes are identified, and the interactions involving Phe are shown to be important in the transcription process. In protein-RNA complexes, Phe is found to occur far less often and is instead replaced by Trp, which binds selectively to C and G, offering a possible mechanism for differentiation between the two nucleic acids. SASA analysis of the two sets of complexes suggests that all of the aromatic amino acids are more heavily involved in binding than would be expected on the balance of probability. Phe and Tyr occur approximately equal in both sets of data, whereas the proportions of His and Trp vary considerably, supporting the idea that these residues may be involved in differentiating between the two nucleic acids.
Citation:
Baker, C.M. and Grant, G.H. (2007) 'Role of aromatic amino acids in protein-nucleic acid recognition', Biopolymers, 85(5-6),pp.456-470.
Publisher:
Wiley-Blackwell
Journal:
Biopolymers
Issue Date:
2007
URI:
http://hdl.handle.net/10547/294682
DOI:
10.1002/bip.20682
PubMed ID:
17219397
Additional Links:
http://www.ncbi.nlm.nih.gov/pubmed/17219397
Type:
Article
Language:
en
ISSN:
0006-3525
Appears in Collections:
Cell and Cryobiology Research Group

Full metadata record

DC FieldValue Language
dc.contributor.authorBaker, Christopher M.en_GB
dc.contributor.authorGrant, Guy H.en_GB
dc.date.accessioned2013-06-26T14:24:09Z-
dc.date.available2013-06-26T14:24:09Z-
dc.date.issued2007-
dc.identifier.citationBaker, C.M. and Grant, G.H. (2007) 'Role of aromatic amino acids in protein-nucleic acid recognition', Biopolymers, 85(5-6),pp.456-470.en_GB
dc.identifier.issn0006-3525-
dc.identifier.pmid17219397-
dc.identifier.doi10.1002/bip.20682-
dc.identifier.urihttp://hdl.handle.net/10547/294682-
dc.description.abstractStatistical analysis of structures from the PBD has been used to examine the role that the aromatic amino acids play in protein-nucleic acid recognition. In protein-DNA complexes, the residues Phe and His are found to bind selectively to the DNA chain--Phe to A and T, and His to T and G. The preferred binding modes are identified, and the interactions involving Phe are shown to be important in the transcription process. In protein-RNA complexes, Phe is found to occur far less often and is instead replaced by Trp, which binds selectively to C and G, offering a possible mechanism for differentiation between the two nucleic acids. SASA analysis of the two sets of complexes suggests that all of the aromatic amino acids are more heavily involved in binding than would be expected on the balance of probability. Phe and Tyr occur approximately equal in both sets of data, whereas the proportions of His and Trp vary considerably, supporting the idea that these residues may be involved in differentiating between the two nucleic acids.en_GB
dc.language.isoenen
dc.publisherWiley-Blackwellen_GB
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pubmed/17219397en_GB
dc.rightsArchived with thanks to Biopolymersen_GB
dc.subject.meshAmino Acids, Aromatic-
dc.subject.meshBinding Sites-
dc.subject.meshDNA-
dc.subject.meshDNA-Binding Proteins-
dc.subject.meshData Interpretation, Statistical-
dc.subject.meshHydrogen Bonding-
dc.subject.meshModels, Molecular-
dc.subject.meshProtein Binding-
dc.subject.meshRNA-
dc.subject.meshRNA-Binding Proteins-
dc.titleRole of aromatic amino acids in protein-nucleic acid recognitionen
dc.typeArticleen
dc.identifier.journalBiopolymersen_GB

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