Critical roles of Asp270 and Trp273 in the α-repeat of the carbohydrate-binding module of endo-1,3-β-glucanase for laminarin-binding avidity.

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Molecular Interactions of β-(1→3)-Glucans with Their Receptors Properties of a family 56 carbohydrate-binding module and its role in the recognition and hydrolysis of β-1,3-glucan.Tryptophan introduction can change β-glucan binding ability of the carbohydrate-binding module of endo-1,3-β-glucanase.

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Critical roles of Asp270 and Trp273 in the α-repeat of the carbohydrate-binding module of endo-1,3-β-glucanase for laminarin-binding avidity.

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2011 nî lūn-bûn

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2011年の論文

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2011年学术文章

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2011年学术文章

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2011年学术文章

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2011年学术文章

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2011年学术文章

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name

Critical roles of Asp270 and T ...... for laminarin-binding avidity.

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Critical roles of Asp270 and T ...... for laminarin-binding avidity.

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type

Item

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Critical roles of Asp270 and T ...... for laminarin-binding avidity.

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Critical roles of Asp270 and T ...... for laminarin-binding avidity.

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prefLabel

Critical roles of Asp270 and T ...... for laminarin-binding avidity.

@en

Critical roles of Asp270 and T ...... for laminarin-binding avidity.

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P1476

Critical roles of Asp270 and T ...... for laminarin-binding avidity.

@en

P2093

Masayuki Oda

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

Nobutoshi Ito

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

Teikichi Ikura

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

Tomonari Tamashiro

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

Yoichi Tanabe

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

P2860

Crystal structures of the sugar complexes of Streptomyces olivaceoviridis E-86 xylanase: sugar binding structure of the family 13 carbohydrate binding module

High-resolution crystal structures of the lectin-like xylan binding domain from Streptomyces lividans xylanase 10A with bound substrates reveal a novel mode of xylan binding

Crystal structures of decorated xylooligosaccharides bound to a family 10 xylanase from Streptomyces olivaceoviridis E-86

The unique binding mode of cellulosomal CBM4 from Clostridium thermocellum cellobiohydrolase A

Site-directed mutagenesis by overlap extension using the polymerase chain reaction

The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling

Carbohydrate-binding modules: fine-tuning polysaccharide recognition

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Mutational analysis of the carbohydrate binding activity of the tobacco lectin

Revisiting the Cellulosimicrobium cellulans yeast-lytic beta-1,3-glucanases toolbox: a review

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s10719-011-9366-x

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77-85

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scholarly article

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10.1007/S10719-011-9366-X

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2011-12-27T00:00:00Z

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Critical roles of Asp270 and Trp273 in the α-repeat of the carbohydrate-binding module of endo-1,3-β-glucanase for laminarin-binding avidity.

about

P2860

P2860

Critical roles of Asp270 and Trp273 in the α-repeat of the carbohydrate-binding module of endo-1,3-β-glucanase for laminarin-binding avidity.

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