Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A metal switch for controlling the activity of molecular motor proteins.

Nature structural & molecular biology - 25 Dec 2011

Cochran Jared C, Zhao Yu Cheng, Wilcox Dean E, Kull F Jon

Abstract excerpt

Kinesins are molecular motors that require a divalent metal ion (for example, Mg(2+)) to convert the energy of ATP hydrolysis into directed force production along microtubules. Here we present the crystal structure of a recombinant kinesin motor domain bound to Mn(2+) and ADP and report on a serine-to-cysteine substitution in the switch 1 motif of kinesin that allows its ATP hydrolysis activity to be controlled...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Diphosphate
Share to Electron Spin Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrolysis

Share to Kinesins

Share to Magnesium

Share to Manganese

Share to Microtubules

Share to Molecular Motor Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 22198464
DOI: 10.1038/nsmb.2190
PMCID: PMC3252401

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A metal switch for controlling the activity of molecular motor proteins.PMID 22198464Read ↗

Structural model for strain-dependent microtubule activation of Mg-ADP release from kinesin.Semantic proximity Read ↗

Kinesin motors as molecular machines.Semantic proximity Read ↗

The structural switch of nucleotide-free kinesin.Semantic proximity Read ↗

Changes in Mg2+ ion concentration and heavy chain phosphorylation regulate the motor activity of a class I myosin.Semantic proximity Read ↗

A kinesin switch I arginine to lysine mutation rescues microtubule function.Semantic proximity Read ↗

A kinesin motor in a force-producing conformation.Semantic proximity Read ↗

The role of ATP hydrolysis for kinesin processivity.Semantic proximity Read ↗

Engineered kinesin motor proteins amenable to small molecule inhibitionSemantic proximity Read ↗

Characterization of kinesin switch I mutations that cause hereditary spastic paraplegia.Semantic proximity Read ↗

Rapid double 8-nm steps by a kinesin mutant.Semantic proximity Read ↗

Molecular motors--a paradigm for mutant analysis.Semantic proximity Read ↗

Decoupling of nucleotide- and microtubule-binding sites in a kinesin mutant.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.