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A fragment activity assay reveals the key residues of TBC1D15 GTPase-activating protein (GAP) in Chi...

A fragment activity assay reveals the key residues of TBC1D15 GTPase-activating protein (GAP) in Chi...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6373008

A fragment activity assay reveals the key residues of TBC1D15 GTPase-activating protein (GAP) in Chiloscyllium plagiosum

About this item

Full title

A fragment activity assay reveals the key residues of TBC1D15 GTPase-activating protein (GAP) in Chiloscyllium plagiosum

Publisher

England: BioMed Central Ltd

Journal title

BMC molecular biology, 2019-02, Vol.20 (1), p.5-5, Article 5

Language

English

Formats

Publication information

Publisher

England: BioMed Central Ltd

More information

Scope and Contents

Contents

GTPase-activating proteins (GAPs) with a TBC (Tre-2/Bub2/Cdc16) domain architecture serve as negative regulators of Rab GTPases. The related crystal structure has been studied and reported by other members of our research group in 2017 (Chen et al. in Protein Sci 26(4):834-846, 2017). The protein crystal structure and sequencing data accession numb...

Alternative Titles

Full title

A fragment activity assay reveals the key residues of TBC1D15 GTPase-activating protein (GAP) in Chiloscyllium plagiosum

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6373008

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6373008

Other Identifiers

ISSN

1471-2199

E-ISSN

1471-2199

DOI

10.1186/s12867-019-0122-2

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