Evidence map›Paper›PMID 23716676›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states.

Chitra A Shintre, Ashley C W Pike, Qiuhong Li, Jung-In Kim, Alastair J Barr, Solenne Goubin, Leela Shrestha, Jing Yang, Georgina Berridge, Jonathan Ross and 10 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.

0numbers the graph read from it
0cells of the map it votes in
122citing papers in PubMed
17.9field-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

122 citing papers in PubMed, 237 citations in OpenAlex.

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

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

20 authors at 3 institutions in 2 countries.

Chitra A ShintreStructural Genomics Consortium, Nuffield Department of Clinical Medicine, University of Oxford, Oxford OX3 7DQ, United Kingdom.
Ashley C W Pike
Qiuhong Li
Jung-In Kim
Alastair J Barr
Solenne Goubin
Leela Shrestha
Jing Yang
Georgina Berridge
Jonathan Ross
Phillip J Stansfeld
Mark S P Sansom
Aled M Edwards
Chas Bountra
Brian D Marsden
Frank von Delft
Alex N Bullock
Opher Gileadi
Nicola A Burgess-Brown
Elisabeth P Carpenter
University of Oxford · GBGenomics (United Kingdom) · GBUniversity of Toronto · CA

Funding

Biotechnology and Biological Sciences Research Council B19456Biotechnology and Biological Sciences Research Council BB/H000267/1Biotechnology and Biological Sciences Research Council BB/I019855/1Biotechnology and Biological Sciences Research Council BBS/B/16011Biotechnology and Biological Sciences Research Council BEP17032CIHRWellcome Trust 092809
6 · The paper itself

Abstract

ABCB10 is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria. In mammals ABCB10 is essential for erythropoiesis, and for protection of mitochondria against oxidative stress. ABCB10 is therefore a potential therapeutic target for diseases in which increased mitochondrial reactive oxygen species production and oxidative stress play a major role. The crystal structure of apo-ABCB10 shows a classic exporter fold ABC transporter structure, in an open-inwards conformation, ready to bind the substrate or nucleotide from the inner mitochondrial matrix or membrane. Unexpectedly, however, ABCB10 adopts an open-inwards conformation when complexed with nonhydrolysable ATP analogs, in contrast to other transporter structures which adopt an open-outwards conformation in complex with ATP. The three complexes of ABCB10/ATP analogs reported here showed varying degrees of opening of the transport substrate binding site, indicating that in this conformation there is some flexibility between the two halves of the protein. These structures suggest that the observed plasticity, together with a portal between two helices in the transmembrane region of ABCB10, assist transport substrate entry into the substrate binding cavity. These structures indicate that ABC transporters may exist in an open-inwards conformation when nucleotide is bound. We discuss ways in which this observation can be aligned with the current views on mechanisms of ABC transporters.

Indexed as

Molecular ConformationProtein Structure, TertiaryAdenosine TriphosphatasesAdenosine TriphosphateAmino Acid SequenceAnimalsATP-Binding Cassette TransportersBinding SitesCrystallography, X-RayHumansLipid BilayersModels, MolecularMolecular Dynamics SimulationMolecular Sequence DataMutationNucleotides1-palmitoyl-2-oleoylphosphatidylcholine1-palmitoyl-2-oleoylphosphatidylethanolamineABCB10 protein, humanAdenosine TriphosphatasesAdenosine TriphosphateATP-Binding Cassette TransportersLipid BilayersNucleotidesPhosphatidylcholinesPhosphatidylethanolaminesABC mitochondrial erythroidcardiolipinhuman membrane protein structurenucleotide complexX-ray crystallography

Identifiers

PMID23716676
PMCPMC3683770
OpenAlexW2022242801

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.