Evidence map›Paper›PMID 10541551›Full record

ArticleGenes & development1999

Crystal structure of an OCA-B peptide bound to an Oct-1 POU domain/octamer DNA complex: specific recognition of a protein-DNA interface.

D Chasman, K Cepek, P A Sharp, 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 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. The Role of the Transcriptional Coactivator BOB.1/OBF.1 in Adaptive Immunity.Advances in experimental medicine and biology · 2024
    Review
  7. Genetic mapping revealsScience immunology · 2023
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Regulation of normal B-cell differentiation and malignant B-cell survival by OCT2.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Review
  18. Article
  19. Article
  20. Article
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

4 authors at 2 institutions in 1 country.

D ChasmanCenter for Cancer Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
K Cepek
P A Sharp
C O Pabo
Center for Cancer Research · USMassachusetts Institute of Technology · US

Funding

VIRUS PRODUCTION COREP30CA014051 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI MATTHEW G. VANDER HEIDEN · 1985 to 2026
$93.9M
USE OF RETROVIRUS PROMOTER TRAP VECTORS TO IDENTIFY ONCOGENES AND ANTI-ONCOGENESP01CA042063 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI JACKS, TYLER E. · 1986 to 2021
$30.5M
CRYSTALLOGRAPHIC STUDY OF REPRESSOR-OPERATOR INTERACTIONR01GM031471 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI PABO, CARL O. · 1985 to 1998
–
NCI NIH HHS P01 CA042063NCI NIH HHS P01-CA42063NCI NIH HHS P30 CA014051NCI NIH HHS P30-CA14051NIGMS NIH HHS GM31471
6 · The paper itself

Abstract

We have determined the crystal structure, at 3.2 A, of a ternary complex containing an OCA-B peptide, the Oct-1 POU domain, and an octamer DNA site. The OCA-B peptide binds in the major groove near the center of the octamer site, and its polypeptide backbone forms a pair of hydrogen bonds with the adenine base at position 5 of the octamer DNA. Numerous protein-protein contacts between the OCA-B peptide and the POU domain are also involved in the ternary complex. In particular, the hydrophobic surface from a short alpha-helix of OCA-B helps to stabilize the complex by binding to a hydrophobic pocket on the POU-specific domain. The structure of this ternary complex is consistent with previous biochemical studies and shows how peptide-DNA and peptide-protein contacts from OCA-B provide structural and functional specificity in the regulation of immunoglobulin transcription.

Indexed as

Amino Acid SequenceAnimalsBase SequenceBinding SitesCrystallography, X-RayDNADNA-Binding ProteinsHost Cell Factor C1HumansMacromolecular SubstancesModels, MolecularMolecular Sequence DataNucleic Acid ConformationOctamer Transcription Factor-1Peptide FragmentsProtein ConformationDNADNA-Binding ProteinsHCFC1 protein, humanHost Cell Factor C1Macromolecular SubstancesOctamer Transcription Factor-1Peptide FragmentsPOU2AF1 protein, humanPOU2F1 protein, humanRecombinant ProteinsTrans-ActivatorsTranscription Factors

Identifiers

PMID10541551
PMCPMC317104
OpenAlexW2079657223

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.