Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mutations in the WFYY motif alter human PrimPol activity: structural insights from atomistic MD simulations.

Physical chemistry chemical physics : PCCP - 15 Jul 2026

Sudhakar Sruthi, Mishra Vipin Kumar, Harikrishna S, Naskar Sumon, Pradeepkumar P I

Abstract excerpt

Human PrimPol (hPrimPol) is the primase and polymerase enzyme involved in reinitiating DNA replication at stalled replication forks. The hPrimPol mutants are linked to multiple ophthalmoplegic conditions and mitochondriopathies. The WFYY motif of hPrimPol was reported to play an essential role in stabilizing the incoming dNTP. Earlier experimental studies reported that the W87G and Y90D mutations significantly...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Motifs
Share to DNA-Directed DNA Polymerase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Primase

Share to Molecular Dynamics Simulation

Share to Multifunctional Enzymes

Share to Mutation

Source

Identifiers

PMID: 42358217
DOI: 10.1039/d6cp00786d

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutations in the WFYY motif alter human PrimPol activity: structural insights from atomistic MD simulations.PMID 42358217Read ↗

Engineering human PrimPol into an efficient RNA-dependent-DNA primase/polymerase.Semantic proximity Read ↗

PrimPol variant V102A with altered primase and polymerase activitiesSemantic proximity Read ↗

Structural insights into inhibition mechanism of the helicase-primase complex from human herpesvirus 1Semantic proximity Read ↗

Crystal structure of the human primase.Semantic proximity Read ↗

The three-component helicase/primase complex of herpes simplex virus-1Semantic proximity Read ↗

Human PrimPol mutation associated with high myopia has a DNA replication defectSemantic proximity Read ↗

Human DNA polymerase delta is a pentameric holoenzyme with dimeric p12 subunit: Implications in enzyme architecture and PCNA interactionSemantic proximity Read ↗

Structural basis of DNA synthesis opposite 8-oxoguanine by human PrimPol primase-polymeraseSemantic proximity Read ↗

Complexed crystal structure of replication restart primosome protein PriB reveals a novel single-stranded DNA-binding mode.Semantic proximity Read ↗

Crystal structure and molecular dynamics of human POLDIP2, a multifaceted adaptor protein in metabolism and genome stabilitySemantic proximity Read ↗

An aromatic-rich loop couples DNA binding and ATP hydrolysis in the PriA DNA helicase.Semantic proximity Read ↗

Helicase‐Primase as a Target of New Therapies for Herpes Simplex Virus InfectionsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.