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

Dynamic Allostery Modulates Catalytic Activity by Modifying the Hydrogen Bonding Network in the Catalytic Site of Human Pin1.

Molecules (Basel, Switzerland) - 15 Jun 2017

Wang Jing, Kawasaki Ryosuke, Uewaki Jun-Ichi, Rashid Arif U R, Tochio Naoya, Tate Shin-Ichi

Abstract excerpt

Allosteric communication among domains in modular proteins consisting of flexibly linked domains with complimentary roles remains poorly understood. To understand how complementary domains communicate, we have studied human Pin1, a representative modular protein with two domains mutually tethered by a flexible linker: a WW domain for substrate recognition and a peptidyl-prolyl isomerase (PPIase) domain. Previous...

Read the complete abstract on PubMed

Topics

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

Share to Catalytic Domain
Share to Histidine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen Bonding

Share to Isomerism

Share to Magnetic Resonance Spectroscopy

Share to NIMA-Interacting Peptidylprolyl Isomerase

Share to Protein Conformation

Share to Protein Structure, Tertiary

Source

Open in PubMed Open full text

Identifiers

PMID: 28617332
DOI: 10.3390/molecules22060992
PMCID: PMC6152768

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dynamic Allostery Modulates Catalytic Activity by Modifying the Hydrogen Bonding Network in the Catalytic Site of Human Pin1.PMID 28617332Read ↗

The C113D mutation in human Pin1 causes allosteric structural changes in the phosphate binding pocket of the PPIase domain through the tug of war in the dual-histidine motif.Semantic proximity Read ↗

Activity and Affinity of Pin1 Variants.Semantic proximity Read ↗

Negative Regulation of Peptidyl-Prolyl Isomerase Activity by Interdomain Contact in Human Pin1.Semantic proximity Read ↗

Allosteric Breakage of the Hydrogen Bond within the Dual-Histidine Motif in the Active Site of Human Pin1 PPIase.Semantic proximity Read ↗

Extended Impact of Pin1 Catalytic Loop Phosphorylation Revealed by S71E Phosphomimetic.Semantic proximity Read ↗

The structural and functional role of the three tryptophan residues in Pin1.Semantic proximity Read ↗

Functionally important residues in the peptidyl-prolyl isomerase Pin1 revealed by unigenic evolution.Semantic proximity Read ↗

Propagated Perturbations from a Peripheral Mutation Show Interactions Supporting WW Domain Thermostability.Semantic proximity Read ↗

The Role of Conformational Dynamics and Allostery in Modulating Protein Evolution.Semantic proximity Read ↗

Conformational Rigidity and Protein Dynamics at Distinct Timescales Regulate PTP1B Activity and Allostery.Semantic proximity Read ↗

Crystallographic proof for an extended hydrogen-bonding network in small prolyl isomerases.Semantic proximity Read ↗

Enhanced Sampling of Interdomain Motion Using Map-Restrained Langevin Dynamics and NMR: Application to Pin1.Semantic proximity Read ↗

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