Lactose Repressor Hinge Domain Independently Binds DNA.

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Lactose Repressor Hinge Domain Independently Binds DNA.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年學術文章

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2018年學術文章

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Lactose Repressor Hinge Domain Independently Binds DNA.

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Lactose Repressor Hinge Domain Independently Binds DNA.

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Lactose Repressor Hinge Domain Independently Binds DNA.

@en

Lactose Repressor Hinge Domain Independently Binds DNA.

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Lactose Repressor Hinge Domain Independently Binds DNA.

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Lactose Repressor Hinge Domain Independently Binds DNA.

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P1476

Lactose Repressor Hinge Domain Independently Binds DNA.

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P2093

Hongli Zhan

http://www.w3.org/2001/XMLSchema#string

Jaskeerat S Gulati

http://www.w3.org/2001/XMLSchema#string

Joseph S Xu

http://www.w3.org/2001/XMLSchema#string

Kathleen S Matthews

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Madeleine N Hewitt

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Matthew A Cruz

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Shirley Liu

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P2860

Structural analysis of lac repressor bound to allosteric effectors

Allostery in the LacI/GalR family: variations on a theme

The solution structure of Lac repressor headpiece 62 complexed to a symmetrical lac operator

A closer view of the conformation of the Lac repressor bound to operator

Crystallographic analysis of Lac repressor bound to natural operator O1

Plasticity in protein-DNA recognition: lac repressor interacts with its natural operator 01 through alternative conformations of its DNA-binding domain.

Mechanism of corepressor-mediated specific DNA binding by the purine repressor

Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by alpha helices

Crystal structure of the lactose operon repressor and its complexes with DNA and inducer

The X-ray structure of the PurR-guanine-purF operator complex reveals the contributions of complementary electrostatic surfaces and a water-mediated hydrogen bond to corepressor specificity and binding affinity

P304

839-847

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P31

scholarly article

P356

10.1002/PRO.3372

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P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P577

2018-02-16T00:00:00Z

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P698

29318690

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P932

5866929

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