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

Hydrophobic Core Variations Provide a Structural Framework for Tyrosine Kinase Evolution and Functional Specialization.

PLoS genetics - 1 Feb 2016

Mohanty Smita, Oruganty Krishnadev, Kwon Annie, Byrne Dominic P, Ferries Samantha, Ruan Zheng, Hanold Laura E, Katiyar Samiksha, Kennedy Eileen J, Eyers Patrick A, Kannan Natarajan

Abstract excerpt

Protein tyrosine kinases (PTKs) are a group of closely related enzymes that have evolutionarily diverged from serine/threonine kinases (STKs) to regulate pathways associated with multi-cellularity. Evolutionary divergence of PTKs from STKs has occurred through accumulation of mutations in the active site as well as in the commonly conserved hydrophobic core. While the functional significance of active site...

Read the complete abstract on PubMed

Topics

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

Share to Aurora Kinase A
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Conserved Sequence

Share to Hydrophobic and Hydrophilic Interactions

Share to Molecular Dynamics Simulation

Share to Protein-Tyrosine Kinases

Share to Receptor Protein-Tyrosine Kinases

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 26925779
DOI: 10.1371/journal.pgen.1005885
PMCID: PMC4771162

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

Hydrophobic Core Variations Provide a Structural Framework for Tyrosine Kinase Evolution and Functional Specialization.PMID 26925779Read ↗

Evolutionary sequence and structural basis for the distinct conformational landscapes of Tyr and Ser/Thr kinases.Semantic proximity Read ↗

Emerging roles of the αC-β4 loop in protein kinase structure, function, evolution, and disease.Semantic proximity Read ↗

The Landscape of Atypical and Eukaryotic Protein Kinases.Semantic proximity Read ↗

Hierarchical organization endows the kinase domain with regulatory plasticitySemantic proximity Read ↗

Kinase regulation by hydrophobic spine assembly in cancer.Semantic proximity Read ↗

HUMAN KINASES DISPLAY MUTATIONAL HOTSPOTS AT COGNATE POSITIONS WITHIN CANCER.Semantic proximity Read ↗

Conservation and divergence in the allosteric architectures of five human protein kinasesSemantic proximity Read ↗

Redistribution of sidechain-sidechain interactions govern ligand-specific binding affinity changes in missense Shank1 PDZ variantsSemantic proximity Read ↗

Congenital disease SNPs target lineage specific structural elements in protein kinases.Semantic proximity Read ↗

Sequence and structure signatures of cancer mutation hotspots in protein kinases.Semantic proximity Read ↗

Allostery is a widespread cause of loss-of-function variant pathogenicity.Semantic proximity Read ↗

Co-evolution of alpha-helical transmembrane protein residues: large-scale variant profiling and complete mutational landscape of 2277 known PDB entries representing 504 unique human protein sequences.Semantic proximity Read ↗

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