Evidence map›Paper›PMID 16500675›Full record

ArticleJournal of molecular biology2006

Crystal structure of the murine cytomegalovirus MHC-I homolog m144.

Kannan Natarajan, Ashleigh Hicks, Janet Mans, Howard Robinson, Rongjin Guan, Roy A Mariuzza, David H Margulies

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

20 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Oncolytic α-herpesvirus and myeloid-tropic cytomegalovirus cooperatively enhance systemic antitumor responses.Molecular therapy : the journal of the American Society of Gene Therapy · 2024
    Article
  3. Review
  4. Review
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  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Self or nonself? That is the question: sensing of cytomegalovirus infection by innate immune receptors.Mammalian genome : official journal of the International Mammalian Genome Society · 2011
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Structural elucidation of the m157 mouse cytomegalovirus ligand for Ly49 natural killer cell receptors.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  20. Review
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 4 institutions in 2 countries.

Kannan NatarajanMolecular Biology Section, Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892-1892, USA.
Ashleigh Hicks
Janet Mans
Howard Robinson
Rongjin Guan
Roy A Mariuzza
David H Margulies
National Institute of Allergy and Infectious Diseases · USAdvanced Bioscience Laboratories (United States) · USBiotechnology Institute · USBrookhaven National Laboratory · US

Funding

STRUCTURE AND FUNCTION OF NATURAL KILLER CELL RECEPTORSR01AI047990 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI MARIUZZA, ROY A · 2000 to 2014
$4.1M
Molecular Interactions Of Lymphoid Cell ReceptorsZ01AI000622 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI MARGULIES, DAVID H. · 1992 to 2008
$3.2M
Intramural NIH HHSNIAID NIH HHS AI 47990NIAID NIH HHS R01 AI047990
6 · The paper itself

Abstract

Large DNA viruses of the herpesvirus family produce proteins that mimic host MHC-I molecules as part of their immunoevasive strategy. The m144 glycoprotein, expressed by murine cytomegalovirus, is thought to be an MHC-I homolog whose expression prolongs viral survival in vivo by preventing natural killer cell activation. To explore the structural basis of this m144 function, we have determined the three-dimensional structure of an m144/beta2-microglobulin (beta2m) complex at 1.9A resolution. This structure reveals the canonical features of MHC-I molecules including readily identifiable alpha1, alpha2, and alpha3 domains. A unique disulfide bond links the alpha1 helix to the beta-sheet floor, explaining the known thermal stability of m144. Close juxtaposition of the alpha1 and alpha2 helices and the lack of critical residues that normally contribute to anchoring the peptide N and C termini eliminates peptide binding. A region of 13 amino acid residues, corresponding to the amino-terminal portion of the alpha2 helix, is missing in the electron density map, suggesting an area of structural flexibility that may be involved in ligand binding.

Indexed as

Amino Acid SequenceAnimalsATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily B, Member 3beta 2-MicroglobulinBinding SitesCarbohydratesCD8 AntigensCell LineCrystallography, X-RayGene ExpressionHistocompatibility Antigens Class IKiller Cells, NaturalLigandsMiceModels, MolecularATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily B, Member 3beta 2-MicroglobulinCarbohydratesCD8 AntigensHistocompatibility Antigens Class ILigandsm144 protein, Mouse cytomegalovirus 1PeptidesTap2 protein, mouseViral Proteins

Identifiers

PMID16500675
PMCPMC1475734
OpenAlexW1969830531

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.