Evidence map›Paper›PMID 10346815›Full record

ArticleGenes & development1999

Crystal structure of the human Pax6 paired domain-DNA complex reveals specific roles for the linker region and carboxy-terminal subdomain in DNA binding.

H E Xu, M A Rould, W Xu, J A Epstein, R L Maas, C O Pabo

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 1999. 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
–field-weighted citation impact
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, 313 citations in OpenAlex.

  1. Review
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  10. Review
  11. Ancestral role of Pax6 in chordate brain regionalization.Frontiers in cell and developmental biology · 2024
    Article
  12. An Unusual Presentation of Novel Missense Variant inCurrent issues in molecular biology · 2023
    Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Overview of theBiophysical reviews · 2021
    Article
  20. Article

63 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

6 authors at 3 institutions in 1 country.

H E XuDepartment of Biology and Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 USA.
M A Rould
W Xu
J A Epstein
R L Maas
C O Pabo
Massachusetts Institute of Technology · USBrigham and Women's Hospital · USHarvard University · US

Funding

The Role of Tdrd7 in Mammalian Lens DevelopmentR01EY010123 · NEI · BRIGHAM AND WOMEN'S HOSPITAL · PI MAAS, RICHARD L · 1993 to 2016
$5.1M
CRYSTALLOGRAPHIC STUDY OF REPRESSOR-OPERATOR INTERACTIONR01GM031471 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI PABO, CARL O. · 1985 to 1998
–
NEI NIH HHS R01 EY010123NEI NIH HHS R01 EY10123NIGMS NIH HHS GM31471
6 · The paper itself

Abstract

Pax6, a transcription factor containing the bipartite paired DNA-binding domain, has critical roles in development of the eye, nose, pancreas, and central nervous system. The 2.5 A structure of the human Pax6 paired domain with its optimal 26-bp site reveals extensive DNA contacts from the amino-terminal subdomain, the linker region, and the carboxy-terminal subdomain. The Pax6 structure not only confirms the docking arrangement of the amino-terminal subdomain as seen in cocrystals of the Drosophila Prd Pax protein, but also reveals some interesting differences in this region and helps explain the sequence specificity of paired domain-DNA recognition. In addition, this structure gives the first detailed information about how the paired linker region and carboxy-terminal subdomain contact DNA. The extended linker makes minor groove contacts over an 8-bp region, and the carboxy-terminal helix-turn-helix unit makes base contacts in the major groove. The structure and docking arrangement of the carboxy-terminal subdomain of Pax6 is remarkably similar to that of the amino-terminal subdomain, and there is an approximate twofold symmetry axis relating the polypeptide backbones of these two helix-turn-helix units. Our structure of the Pax6 paired domain-DNA complex provides a framework for understanding paired domain-DNA interactions, for analyzing mutations that map in the linker and carboxy-terminal regions of the paired domain, and for modeling protein-protein interactions of the Pax family proteins.

Indexed as

Crystallography, X-RayHomeodomain ProteinsAmino Acid SequenceDNADNA-Binding ProteinsEye ProteinsHelix-Turn-Helix MotifsHumansModels, GeneticModels, MolecularMolecular Sequence DataMutation, MissenseNucleic Acid ConformationPaired Box Transcription FactorsPAX6 Transcription FactorProtein BindingDNADNA-Binding ProteinsEye ProteinsHomeodomain ProteinsPaired Box Transcription FactorsPAX6 protein, humanPAX6 Transcription FactorRepressor Proteins

Identifiers

PMID10346815
PMCPMC316729
OpenAlexW2070250500

What OpenQuestion holds

Textmetadata
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Registered trials

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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.