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Structure of the SMYD2-PARP1 Complex Reveals Both Productive and Allosteric Modes of Peptide Binding

bioRxiv (Cold Spring Harbor Laboratory)(2024)10.1101/2024.12.03.626679Source: DataRank Database

Structure of the SMYD2-PARP1 Complex Reveals Both Productive and Allosteric Modes of Peptide Binding is a research paper published in bioRxiv (Cold Spring Harbor Laboratory) (2024). On theSindex it has a DataRank of 0.

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Authors (14)

Eid Alshammari ORCID,Jacob Sobota,Nicolas Spellmon,Emerson Perry,Tianxin Cao

Live enrichment

PubMed:39677743 OpenAlex:https://openalex.org/W4405006861

National Institutes of Health

Grant: 1R01HL128647-01

Chemokine Signaling in EPC Angiogenesis: A Role of Lysine Methylation

NHLBI NIH HHS

Grant: R01 HL128647

greenLicense: cc-by

repositoryhttps://doi.org/10.1101/2024.12.03.626679

GREENhttps://doi.org/10.1101/2024.12.03.626679

repositoryhttps://doi.org/10.1101/2024.12.03.626679

publisherhttps://syndication.highwire.org/content/doi/10.1101/2024.12.03.626679

repositoryhttps://pubmed.ncbi.nlm.nih.gov/39677743

Fields of Study

Cancer-related gene regulationEpigenetics and DNA MethylationGenomics and Chromatin DynamicsMedicineBiologyChemistry0301 basic medicine03 medical and health sciences

Keywords

Allosteric regulationCooperativityAllosteric enzymeBinding siteBiophysicsMethyltransferaseLysineActive siteProtein structureHistoneCooperative bindingPlasma protein bindingBiologyEnzymeChemistryComputational biologyBiochemistryAmino acidDNAArticleProtein methylationSMYD proteinsStructural biologyX-ray crystallography

Sustainable Development Goals

SDG 0: Life in Land