Publication Date:
1999-06-05
Description:
The papillomavirus E2 protein regulates viral transcription and DNA replication through interactions with cellular and viral proteins. The amino-terminal activation domain, which represents a protein class whose structural themes are poorly understood, contains key residues that mediate these functional contacts. The crystal structure of a protease-resistant core of the human papillomavirus type 18 E2 activation domain reveals a novel fold creating a cashew-shaped form with a glutamine-rich alpha helix packed against a beta-sheet framework. The protein surface shows extensive overlap of determinants for replication and transcription. The structure broadens the concept of activators to include proteins with potentially malleable, but certainly ordered, structures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harris, S F -- Botchan, M R -- CA30490/CA/NCI NIH HHS/ -- CA42414/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1999 Jun 4;284(5420):1673-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3204, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10356398" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Amino Acid Substitution
;
Crystallization
;
Crystallography, X-Ray
;
DNA Replication
;
Evolution, Molecular
;
Humans
;
Models, Molecular
;
Molecular Sequence Data
;
Oncogene Proteins, Viral/*chemistry/physiology
;
Papillomaviridae/*chemistry/physiology
;
Protein Conformation
;
Protein Folding
;
Protein Structure, Secondary
;
Trans-Activators/*chemistry/physiology
;
Virus Replication
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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