Evidence map›Paper›PMID 14645714›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

Structural basis of peptide-carbohydrate mimicry in an antibody-combining site.

Nand K Vyas, Meenakshi N Vyas, Mary C Chervenak, David R Bundle, B Mario Pinto, Florante A Quiocho

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
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  11. A peptide inhibitor of HIV-1 neutralizing antibody 2G12 is not a structural mimic of the natural carbohydrate epitope on gp120.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2008
    Article
  12. The epitope space of the human proteome.Protein science : a publication of the Protein Society · 2008
    Article
  13. Review
  14. Article
  15. Article
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  19. 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

6 authors.

Nand K VyasDepartment of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.
Meenakshi N Vyas
Mary C Chervenak
David R Bundle
B Mario Pinto
Florante A Quiocho

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The structure of a complex between the Fab fragment of the antibody (SYA/J6) specific for the cell surface O-antigen polysaccharide of the pathogen Shigella flexneri Y and an octapeptide (Met-Asp-Trp-Asn-Met-His-Ala-Ala), a functional mimic of the O-antigen, has been determined at 1.8-A resolution. Comparison of the structure with that of the complex with the pentasaccharide antigen [-->2)-alpha-L-Rha-(1-->2)-alpha-L-Rha-(1-->3)-alpha-L-Rha-(1-->3)-beta-D-GlcNAc-(1-->2)-alpha-L-Rha-(1-->] reveals the molecular recognition process by which a peptide mimics a carbohydrate in binding to an antibody. The binding modes of the two ligands differ considerably. Octapeptide binding complements the shape of the combining site groove much better than pentasaccharide binding. Moreover, the peptide makes a much greater number of contacts (126), which are mostly van der Waals interactions, with the Fab than the saccharide (74). An unusual feature is also the involvement of 12 water molecules in mediating hydrogen bonds between residues within the peptide or of the peptide and Fab. Despite better shape complementarity and greater number of contacts, the octapeptide binds with an affinity (KA = 2.5 x 10(5) M-1, measured by calorimetry) only approximately 2-fold tighter than the pentasaccharide. The structural results are relevant to the design of peptide mimetics with improved affinity for use as vaccines.

Indexed as

Binding Sites, AntibodyAnimalsBinding SitesCalorimetryCarbohydratesCrystallography, X-RayHydrogen BondingImmunoglobulin Fab FragmentsKineticsLigandsMiceModels, MolecularOligosaccharidesPeptidesShigella flexneriCarbohydratesImmunoglobulin Fab FragmentsLigandsOligosaccharidesPeptides

Identifiers

PMID14645714
PMCPMC299889

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.