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Article

A novel kinase mutation in VEGFR-1 predisposes its αC-helix/activation loop towards allosteric activation: Atomic insights from protein simulation.

European journal of human genetics : EJHG - 1 Aug 2016

Mokhdomi Taseem A, Bukhari Shoiab, Chikan Naveed Anjum, Amin Asif, Wafai Asrar H, Wani Sajad H, Chowdri Nisar A, Qadri Raies A

Abstract excerpt

Vascular endothelial growth factor receptor 1 (VEGFR-1) has been implicated in diverse pathologies, including cancers. Although VEGFR-1 is considered as functionally impaired kinase, its decoy characteristics make it an important regulator of VEGFR-mediated signaling, particularly in tumor angiogenesis. VEGFR-1 conveys signaling via its tyrosine kinase (TK) domain whose activation is regulated by phosphorylation...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Mutation, Missense

Share to Protein Conformation, alpha-Helical

Share to Protein Processing, Post-Translational

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Source

Open in PubMed Open full text

Identifiers

PMID: 27049304
DOI: 10.1038/ejhg.2016.26
PMCID: PMC4989210

Variants

rs730882263

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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