Binding of human SWI1 ARID domain to DNA without sequence specificity: A molecular dynamics study / 华中科技大学学报(医学)(英德文版)
Journal of Huazhong University of Science and Technology (Medical Sciences)
; (6): 469-476, 2015.
Article
em En
| WPRIM
| ID: wpr-250393
Biblioteca responsável:
WPRO
ABSTRACT
SWI1 is a member of a new class of tumor DNA-binding proteins named as the AT-rich interaction domain family (ARID), and considered to bind with AT base pairs specifically. Genomic and functional data support ARID1A as a tumor suppressor because ARID1A/BAF250a (SWI1) subunit of the SWI/SNF chromatin-remodeling complex has emerged as recurrently mutated in a broad array of tumor types. But the crystal structure of SWI1 has not been solved as yet. Using docking and molecular dynamics, we predicted the DNA interaction pattern of human SWI1 ARID and made comparisons with the other two representative ARID family members, human Mrf-2 ARID and Drosophila Dri ARID. Dynamic results revealed that the N-terminal and loop L1 of SWI1 ARID bound with the DNA major groove, while the loop L2 and helix H6 bound with the minor groove. Moreover, it was found that SWI1 ARID bound with DNA apparently in a sequence-nonspecific manner. It was concluded that SWI1 ARID can form stable complex with sequence-nonspecific DNA segment comparing to Mrf-2 ARID/DNA and Dri ARID/DNA sequence-specific complexes.
Texto completo:
1
Índice:
WPRIM
Assunto principal:
Fatores de Transcrição
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Sítios de Ligação
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DNA
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Proteínas Nucleares
/
Modelos Moleculares
/
Química
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Estrutura Terciária de Proteína
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Proteínas de Homeodomínio
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Proteínas de Drosophila
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Proteínas de Ligação a DNA
Tipo de estudo:
Prognostic_studies
Limite:
Humans
Idioma:
En
Revista:
Journal of Huazhong University of Science and Technology (Medical Sciences)
Ano de publicação:
2015
Tipo de documento:
Article