Evidence map›Paper›PMID 20089642›Full record

ArticleJournal of virology2010

Structure function studies of vaccinia virus host range protein k1 reveal a novel functional surface for ankyrin repeat proteins.

Yongchao Li, Xiangzhi Meng, Yan Xiang, Junpeng Deng

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
0.4field-weighted citation impact, top 42% 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

23 citing papers in PubMed, 34 citations in OpenAlex.

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  15. Deletion of theJournal of virology · 2017
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  17. Structural basis for antagonizing a host restriction factor by C7 family of poxvirus host-range proteins.Proceedings of the National Academy of Sciences of the United States of America · 2015
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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

4 authors at 2 institutions in 1 country.

Yongchao LiDepartment of Microbiology and Immunology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Dr., San Antonio, TX 78229, USA.
Xiangzhi Meng
Yan Xiang
Junpeng Deng
The University of Texas Health Science Center at San Antonio · USOklahoma State University · US

Funding

Poxvirus Immune Evasion MechanismsR01AI079217 · NIAID · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI XIANG, YAN · 2008 to 2018
$3.3M
Structure-function studies on IL-18, IL-18 binding proteins and receptorsR01AI081928 · NIAID · OKLAHOMA STATE UNIVERSITY STILLWATER · PI DENG, JUNPENG · 2009 to 2012
$1.3M
Molecular Mechanism of Poxvirus Host Range GenesR21AI065731 · NIAID · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI XIANG, YAN · 2007 to 2008
$398k
NIAID NIH HHS AI065731NIAID NIH HHS AI079217NIAID NIH HHS AI081928NIAID NIH HHS R01 AI079217NIAID NIH HHS R01 AI081928NIAID NIH HHS R21 AI065731
6 · The paper itself

Abstract

Poxvirus host tropism at the cellular level is regulated by virus-encoded host range proteins acting downstream of virus entry. The functioning mechanisms of most host range proteins are unclear, but many contain multiple ankyrin (ANK) repeats, a motif that is known for ligand interaction through a concave surface. We report here the crystal structure of one of the ANK repeat-containing host range proteins, the vaccinia virus K1 protein. The structure, at a resolution of 2.3 A, showed that K1 consists entirely of ANK repeats, including seven complete ones and two incomplete ones, one each at the N and C terminus. Interestingly, Phe82 and Ser83, which were previously shown to be critical for K1's function, are solvent exposed and located on a convex surface, opposite the consensus ANK interaction surface. The importance of this convex surface was further supported by our additional mutagenesis studies. We found that K1's host range function was negatively affected by substitution of either Asn51 or Cys47 and completely abolished by substitution of both residues. Cys47 and Asn51 are also exposed on the convex surface, spatially adjacent to Phe82 and Ser83. Altogether, our data showed that K1 residues on a continuous convex ANK repeat surface are critical for the host range function, suggesting that K1 functions through ligand interaction and does so with a novel ANK interaction surface.

Indexed as

Ankyrin RepeatAmino Acid SequenceAnimalsChlorocebus aethiopsHeLa CellsHumansMolecular Sequence DataNF-kappa BProtein Structure, SecondaryStructure-Activity RelationshipVero CellsViral ProteinsK1L protein, Vaccinia virusNF-kappa BViral Proteins

Identifiers

PMID20089642
PMCPMC2838116
OpenAlexW2143306199

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.