Evidence map›Paper›PMID 20399181›Full record

ArticleStructure (London, England : 1993)2010

Structure of concatenated HAMP domains provides a mechanism for signal transduction.

Michael V Airola, Kylie J Watts, Alexandrine M Bilwes, Brian R Crane

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
8.5field-weighted citation impact, top 2% 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

76 citing papers in PubMed, 146 citations in OpenAlex.

  1. Conformational diversity in poly-HAMP arrays and its implications for signal transduction.Protein science : a publication of the Protein Society · 2026
    Article
  2. Signaling mechanism of the transmembrane energy receptor Aer.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. A Designed ZnJournal of the American Chemical Society · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. AlphaFold2 captures the conformational landscape of the HAMP signaling domain.Protein science : a publication of the Protein Society · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Protein design-scapes generated by microfluidic DNA assembly elucidate domain coupling in the bacterial histidine kinase CpxA.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  17. Microbiology and molecular biology reviews : MMBR · 2021
    Review
  18. Coiled-Coil Based Inclusion Bodies and Their Potential Applications.Frontiers in bioengineering and biotechnology · 2021
    Review
  19. Article
  20. Interface switch mediates signal transmission in a two-component system.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article

16 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

4 authors at 1 institution in 1 country.

Michael V AirolaDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
Kylie J Watts
Alexandrine M Bilwes
Brian R Crane
Cornell University · US

Funding

TRAINING IN MOLECULAR PHYSICS OF BIOLOGICAL SYSTEMST32GM008267 · NIGMS · CORNELL UNIVERSITY ITHACA · PI WANG, MICHELLE D. · 1988 to 2021
$9.6M
The Structure and Function of the Bacterial ChemosomeR01GM066775 · NIGMS · CORNELL UNIVERSITY ITHACA · PI CRANE, BRIAN R · 2003 to 2016
$4.3M
SENSORY TRANSDUCTION IN BACTERIAR01GM029481 · NIGMS · LOMA LINDA UNIVERSITY · PI TAYLOR, BARRY L · 1985 to 2011
$2.9M
NIGMS NIH HHS GM029481NIGMS NIH HHS GM066775NIGMS NIH HHS GM08267NIGMS NIH HHS R01 GM029481NIGMS NIH HHS R01 GM066775NIGMS NIH HHS T32 GM008267
6 · The paper itself

Abstract

HAMP domains are widespread prokaryotic signaling modules found as single domains or poly-HAMP chains in both transmembrane and soluble proteins. The crystal structure of a three-unit poly-HAMP chain from the Pseudomonas aeruginosa soluble receptor Aer2 defines a universal parallel four-helix bundle architecture for diverse HAMP domains. Two contiguous domains integrate to form a concatenated di-HAMP structure. The three HAMP domains display two distinct conformations that differ by changes in helical register, crossing angle, and rotation. These conformations are stabilized by different subsets of conserved residues. Known signals delivered to HAMP would be expected to switch the relative stability of the two conformations and the position of a coiled-coil phase stutter at the junction with downstream helices. We propose that the two conformations represent opposing HAMP signaling states and suggest a signaling mechanism whereby HAMP domains interconvert between the two states, which alternate down a poly-HAMP chain.

Indexed as

Protein Structure, TertiaryAmino Acid SequenceComputational BiologyModels, MolecularMolecular ConformationMolecular Sequence DataProtein ConformationProteinsProtein Structure, SecondaryPseudomonas aeruginosaSelenomethionineSequence Homology, Amino AcidSignal TransductionSolventsProteinsSelenomethionineSolvents

Identifiers

PMID20399181
PMCPMC2892831
OpenAlexW2138243191

What OpenQuestion holds

Textmetadata
LicenceTDM
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.