Cwp84, a Clostridium difficile cysteine protease, exhibits conformational flexibility in the absence of its propeptide.

about

An update on antibody-based immunotherapies for Clostridium difficile infection The structure of the S-layer of Clostridium difficile.The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile.

P2860

Q26740788-9C665056-5D34-43C8-9200-11D96E0DE099 Q47369077-B71C87EB-917A-44B7-9474-6DDE7E3F6BC3 Q47588518-EFC6F1DA-DFBC-47FC-8B86-CE96D0B620A8

P2860

Cwp84, a Clostridium difficile cysteine protease, exhibits conformational flexibility in the absence of its propeptide.

Item

http://www.wikidata.org/entity/Q41437831

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

@zh-cn

name

Cwp84, a Clostridium difficile ...... the absence of its propeptide.

@en

type

Item

label

Cwp84, a Clostridium difficile ...... the absence of its propeptide.

@en

prefLabel

Cwp84, a Clostridium difficile ...... the absence of its propeptide.

@en

P1476

Cwp84, a Clostridium difficile ...... the absence of its propeptide

@en

P2093

April K Roberts

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

Clifford C Shone

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

P2860

Structural basis for the recognition and cleavage of histone H3 by cathepsin L

Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment

MolProbity: all-atom structure validation for macromolecular crystallography

The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity

The structure of a thermostable mutant of pro-papain reveals its activation mechanism

The structure of the cysteine protease and lectin-like domains of Cwp84, a surface layer-associated protein fromClostridium difficile

Structure of papain refined at 1.65 A resolution

Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide

Crystal structure of the wild-type human procathepsin B at 2.5 A resolution reveals the native active site of a papain-like cysteine protease zymogen

XDS

P304

295-303

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

P31

scholarly article

P356

10.1107/S2053230X15001065

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

P433

Pt 3

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

P478

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

P50

William J. Bradshaw

K. Ravi Acharya

P577

2015-02-19T00:00:00Z

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

P5875

273445451

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

P698

25760704

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

P921

Clostridium difficile

P932

4356305

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

Cwp84, a Clostridium difficile cysteine protease, exhibits conformational flexibility in the absence of its propeptide.

about

P2860

P2860

Cwp84, a Clostridium difficile cysteine protease, exhibits conformational flexibility in the absence of its propeptide.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P921

P932