Evidence map›Paper›PMID 8606780›Full record

ArticleNature1996

Crystal structure of the motor domain of the kinesin-related motor ncd.

E P Sablin, F J Kull, R Cooke, R D Vale, R J Fletterick

Abstract read
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In one paragraph

Article in Nature, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing papers in PubMed
16.4field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

123 citing papers in PubMed, 353 citations in OpenAlex.

  1. Review
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  4. Tether-scanning the kinesin motor domain reveals a core mechanical action.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  15. Synthetic-Evolution Reveals Narrow Paths to Regulation of theInternational journal of biological sciences · 2019
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  16. Review
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  19. Article
  20. Molecular origin of the weak susceptibility of kinesin velocity to loads and its relation to the collective behavior of kinesins.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article

63 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

E P SablinDepartment of Biochemistry/Biophysics, University of California, San Francisco, California 94143, USA.
F J Kull
R Cooke
R D Vale
R J Fletterick
University of California, San Francisco · USHoward Hughes Medical Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microtubule-based ATPases of the kinesin superfamily provide the motile force for many animated features of living cells. Kinesin motors differ in their direction of movement along microtubules. Kinesin and ncd, a kinesin-related motor involved in formation and maintenance of mitotic and meiotic spindles, move in opposite directions along microtubules, even though their motor domains are 40% identical in amino-acid sequence. Here we report the crystal structure of the MgADP complex of the Drosophila ncd motor domain determined to 2.5A by X-ray crystallography, and compare it to the kinesin structure. The ncd and kinesin motor domains are remarkably similar in structure, and the locations of conserved surface amino acids suggest these motors share a common microtubule-binding site. Moreover, structural and functional comparisons of ncd, kinesin, myosin and G proteins indicate that these NTPases may have a similar strategy of changing conformation between NTP and NDP states. We propose a general model for converting a common gamma-phosphate-sensing mechanism into opposite polarities of movement for kinesin and ncd.

Indexed as

Drosophila ProteinsAdenosine DiphosphateAmino Acid SequenceAnimalsConserved SequenceCrystallography, X-RayDrosophilaKinesinsMicrotubule ProteinsModels, MolecularMolecular Sequence DataProtein ConformationSequence Homology, Amino AcidStructure-Activity RelationshipAdenosine DiphosphateDrosophila ProteinsKinesinsMicrotubule Proteinsncd protein, Drosophila

Identifiers

PMID8606780
OpenAlexW2033276495

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.