Evidence map›Paper›PMID 17426136›Full record

ArticleNucleic acids research2007

Crystal structure of the third KH domain of human poly(C)-binding protein-2 in complex with a C-rich strand of human telomeric DNA at 1.6 A resolution.

Sebastian Fenn, Zhihua Du, John K Lee, Richard Tjhen, Robert M Stroud, Thomas L James

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

27 citing papers in PubMed, 42 citations in OpenAlex.

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  19. Mutation and crystallization of the first KH domain of human polycytosine-binding protein 1 (PCBP1) in complex with DNA.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011
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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 1 institution in 1 country.

Sebastian FennDepartment of Pharmaceutical Chemistry, University of California, San Francisco, California 94143-2280, USA.
Zhihua Du
John K Lee
Richard Tjhen
Robert M Stroud
Thomas L James
University of California, San Francisco · US

Funding

THREE DIMENSIONAL HIV RNA GENOME TARGETED DRUG LEADSR01AI046967 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI JAMES, THOMAS L · 2000 to 2011
$4.1M
TRNA METHYLASE AND TRNA PSEUDOURIDINE SYNTHASER01GM051232 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 1996 to 2012
$3.4M
NIAID NIH HHS AI46967NIAID NIH HHS R01 AI046967NIGMS NIH HHS GM51232NIGMS NIH HHS R01 GM051232
6 · The paper itself

Abstract

KH (hnRNP K homology) domains, consisting of approximately 70 amino acid residues, are present in a variety of nucleic-acid-binding proteins. Among these are poly(C)-binding proteins (PCBPs), which are important regulators of mRNA stability and posttranscriptional regulation in general. All PCBPs contain three different KH domains and recognize poly(C)-sequences with high affinity and specificity. To reveal the molecular basis of poly(C)-sequence recognition, we have determined the crystal structure, at 1.6 A resolution, of PCBP2 KH3 domain in complex with a 7-nt DNA sequence (5'-AACCCTA-3') corresponding to one repeat of the C-rich strand of human telomeric DNA. The domain assumes a type-I KH fold in a betaalphaalphabetabetaalpha configuration. The protein-DNA interface could be studied in unprecedented detail and is made up of a series of direct and water-mediated hydrogen bonds between the protein and the DNA, revealing an especially dense network involving several structural water molecules for the last 2 nt in the core recognition sequence. Unlike published KH domain structures, the protein crystallizes without protein-protein contacts, yielding new insights into the dimerization properties of different KH domains. A nucleotide platform, an interesting feature found in some RNA molecules, was identified, evidently for the first time in DNA.

Indexed as

Models, MolecularAmino Acid SequenceBinding SitesCrystallography, X-RayDNAHumansHydrogen BondingMolecular Sequence DataProtein Structure, TertiaryRNA-Binding ProteinsSequence AlignmentTelomereDNAPCBP2 protein, humanRNA-Binding Proteins

Identifiers

PMID17426136
PMCPMC1885661
OpenAlexW2101175599

What OpenQuestion holds

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LicenceCC BY-NC
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.