Evidence map›Paper›PMID 19396172›Full record

ArticleNature structural & molecular biology2009

Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsis.

Fang Fang Yin, Scott Bailey, C Axel Innis, Mihai Ciubotaru, Satwik Kamtekar, Thomas A Steitz, David G Schatz

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

61 citing papers in PubMed, 92 citations in OpenAlex.

  1. Characterization of immunoglobulin loci inNAR genomics and bioinformatics · 2026
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  13. Targeting HMGB3/hTERT axis for radioresistance in cervical cancer.Journal of experimental & clinical cancer research : CR · 2020
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  20. Article

1 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

7 authors at 2 institutions in 1 country.

Fang Fang YinDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, USA.
Scott Bailey
C Axel Innis
Mihai Ciubotaru
Satwik Kamtekar
Thomas A Steitz
David G Schatz
Yale University · USHoward Hughes Medical Institute · US

Funding

PREDOCTORAL PROGRAM IN BIOPHYSICST32GM008283 · NIGMS · YALE UNIVERSITY · PI XIONG, YONG · 1988 to 2022
$10.5M
Mechanism and Targeting of V(D)J RecombinationR01AI032524 · NIAID · YALE UNIVERSITY · PI David G. Schatz · 1992 to 2026
$6.7M
Immunoglobulin and T Cell Receptor Gene AssemblyR37AI032524 · NIAID · YALE UNIVERSITY · PI SCHATZ, DAVID G. · 2007 to 2016
$3.5M
Howard Hughes Medical InstituteNIAID NIH HHS AI32524NIAID NIH HHS R01 AI032524NIAID NIH HHS R37 AI032524NIGMS NIH HHS T32 GM008283NIGMS NIH HHS T32 GM08283
6 · The paper itself

Abstract

The products of recombination-activating genes RAG1 and RAG2 mediate the assembly of antigen receptor genes during lymphocyte development in a process known as V(D)J recombination. Lack of structural information for the RAG proteins has hindered mechanistic studies of this reaction. We report here the crystal structure of an essential DNA binding domain of the RAG1 catalytic core bound to its nonamer DNA recognition motif. The RAG1 nonamer binding domain (NBD) forms a tightly interwoven dimer that binds and synapses two nonamer elements, with each NBD making contact with both DNA molecules. Biochemical and biophysical experiments confirm that the two nonamers are in close proximity in the RAG1/2-DNA synaptic complex and demonstrate the functional importance of the protein-DNA contacts revealed in the structure. These findings reveal a previously unsuspected function for the NBD in DNA synapsis and have implications for the regulation of DNA binding and cleavage by RAG1 and RAG2.

Indexed as

Chromosome PairingProtein MultimerizationAmino Acid MotifsAmino Acid SequenceAnimalsBase SequenceCrystallography, X-RayDNAFluorescence Resonance Energy TransferHomeodomain ProteinsMiceModels, MolecularMolecular Sequence DataNucleic Acid ConformationProtein Structure, QuaternaryProtein Structure, TertiaryDNAHomeodomain ProteinsRAG-1 proteinSolutions

Identifiers

PMID19396172
PMCPMC2715281
OpenAlexW1977764826

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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.