Evidence map›Paper›PMID 28841430›Full record

ReviewCurrent opinion in structural biology2017

Evolution of protein specificity: insights from ancestral protein reconstruction.

Mohammad A Siddiq, Georg Ka Hochberg, Joseph W Thornton

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

62 citing papers in PubMed, 111 citations in OpenAlex.

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  18. Evolution and diversification of carboxylesterase-like [4+2] cyclases in aspidosperma and iboga alkaloid biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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  20. Article

2 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

3 authors at 1 institution in 1 country.

Mohammad A SiddiqDepartment of Ecology and Evolution, University of Chicago, USA.
Georg Ka HochbergDepartment of Ecology and Evolution, University of Chicago, USA.
Joseph W ThorntonDepartment of Ecology and Evolution, University of Chicago, USA; Department of Human Genetics, University of Chicago, USA. Electronic address: joet1@uchicago.edu.
University of Chicago · US

Funding

PREDOCTORAL TRAINING IN GENETICS AND REGULATIONT32GM007197 · NIGMS · UNIVERSITY OF CHICAGO · PI ROTHMAN-DENES, LUCIA B. B · 1985 to 2020
$17.0M
Mechanisms for the evolution of novel DNA specificity in a transcription factor fR01GM104397 · NIGMS · UNIVERSITY OF CHICAGO · PI THORNTON, JOSEPH W · 2013 to 2016
$1.3M
Deep characterization of the sequence space and evolutionary trajectories of reconstructed ancestral proteins - Resubmission 01R01GM121931 · NIGMS · UNIVERSITY OF CHICAGO · PI THORNTON, JOSEPH W · 2017 to 2020
$1.3M
NIGMS NIH HHS R01 GM104397NIGMS NIH HHS R01 GM121931NIGMS NIH HHS T32 GM007197
6 · The paper itself

Abstract

Specific interactions between proteins and their molecular partners drive most biological processes, so understanding how these interactions evolve is an important question for biochemists and evolutionary biologists alike. It is often thought that ancestral proteins were systematically more promiscuous than modern proteins and that specificity usually evolves after gene duplication by partitioning and refining the activities of multifunctional ancestors. However, recent studies using ancestral protein reconstruction (APR) have found that ligand-specific functions in some modern protein families evolved de novo from ancestors that did not already have those functions. Further, the new specific interactions evolved by simple mechanisms, with just a few mutations changing classically recognized biochemical determinants of specificity, such as steric and electrostatic complementarity. Acquiring new specific interactions during evolution therefore appears to be neither difficult nor rare. Rather, it is likely that proteins continually gain and lose new activities over evolutionary time as mutations cause subtle but consequential changes in the shape and electrostatics of interaction interfaces. Only a few of these activities, however, are incorporated into the biological processes that contribute to fitness before they are lost to the ravages of further mutation.

Indexed as

Evolution, MolecularAllosteric RegulationEnzymesLigandsMetabolic Networks and PathwaysProtein BindingProteinsStructure-Activity RelationshipSubstrate SpecificityEnzymesLigandsProteins

Identifiers

PMID28841430
PMCPMC6141201
OpenAlexW2746980362

What OpenQuestion holds

Textmetadata
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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.