The role of conserved histidines in the structure and stability of human papillomavirus type 16 E2 DNA-binding domain.

The role of conserved histidines in the structure and stability of human papillomavirus type 16 E2 DNA-binding domain. Research Abstract Details 

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The role of conserved histidines in the structure and stability of human papillomavirus type 16 E2 DNA-binding domain. Abstract Text:

Kakoli Bose,Nicholas C Yoder,Krishna Kumar,James D Baleja,

The E2 protein of papillomavirus is the key regulator of viral transcription and replication. Dimerization, which takes place via its conserved C-terminal DNA-binding domain (DBD), is critical for these functions. The presence and conservation of two histidines (H290 and H320) at or near the dimer interface suggests the importance of their roles in protein structure and stability that was explored by mutating them to neutral alanine. The H290A mutant but not the H320A mutant showed a significant change in the secondary as well as tertiary structure, as monitored by far- and near-UV circular dichroism and fluorescence. We show that the wild-type DBD was more stable than either of the two histidine mutants at pH 7.5 but that the order of stability changed with pH, where, at pH 4.5, the H290A mutant was most stable. Although H290 is important for pH dependence of the stability, it is not critical for dimerization or folding. The determination of pKa values for the solvent-exposed histidine residues shows that the surface properties of the protein change with pH, suggesting different interactions that can be made by the protein in response to cellular acidification. Moreover, identification of residues crucial for E2 stability will help in the design of modified proteins with desired characteristics.

The role of conserved histidines in the structure and stability of human papillomavirus type 16 E2 DNA-binding domain. Publishing Authors By Initials

K Bose,NC Yoder,K Kumar,JD Baleja,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: protein folding research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: protein folding research

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The role of conserved histidines in the structure and stability of human papillomavirus type 16 E2 DNA-binding domain. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Biochemistry

VOLUME: 46

Page Numbers: 1402-11

Journal Abbreviation: Biochemistry

ISSN: 0006-2960

DAY: 6

MONTH: Feb

YEAR: 2007

The role of conserved histidines in the structure and stability of human papillomavirus type 16 E2 DNA-binding domain. Information

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LANGUAGE: eng

NlmUniqueID: 370623

The role of conserved histidines in the structure and stability of human papillomavirus type 16 E2 DNA-binding domain. Keywords Mesh Terms:

KEYWORDS: Protein Folding

MESH TERMS: chemistry

Chemical & Substance for Abstract: The role of conserved histidines in the structure and stability of human papillomavirus type 16 E2 DNA-binding domain. Information

Substance Name: Histidine

Registry Number: 71-00-1

Grant and Affiliation Information for The role of conserved histidines in the structure and stability of human papillomavirus type 16 E2 DNA-binding domain.

AFFILIATION: Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.

Country: United States

AGENCY: United States NCRR

GRANT: S10RR017948

ACRONYM: RR

MEDLINETA: Biochemistry

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