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Insights into dynein motor domain function from a 3.3-Å crystal structure

Insights into dynein motor domain function from a 3.3-Å crystal structure

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3393637

Insights into dynein motor domain function from a 3.3-Å crystal structure

About this item

Full title

Insights into dynein motor domain function from a 3.3-Å crystal structure

Publisher

New York: Nature Publishing Group US

Journal title

Nature structural & molecular biology, 2012-05, Vol.19 (5), p.492-497

Language

English

Formats

Publication information

Publisher

New York: Nature Publishing Group US

More information

Scope and Contents

Contents

Dynein is a molecular motor involved in many cellular functions. The motor domain of dynein contains six AAA+ domains forming a ring that interacts with the motile linker domain. The structure of yeast dynein motor domain crystallized without nucleotides is now presented at 3.3-Å resolution and shows the specific contacts between linker and ring, w...

Alternative Titles

Full title

Insights into dynein motor domain function from a 3.3-Å crystal structure

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3393637

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3393637

Other Identifiers

ISSN

1545-9993

E-ISSN

1545-9985

DOI

10.1038/nsmb.2272

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