NMR resonance assignment of a ligand-binding domain of ephrin receptor A2.

IF 0.8 4区生物学 Q4 BIOPHYSICS

Biomolecular NMR Assignments Pub Date : 2024-12-19 DOI:10.1007/s12104-024-10211-4

Konstantin S Mineev, Santosh L Gande, Verena Linhard, Sattar Khashkhashi Moghaddam, Harald Schwalbe

引用次数: 0

Abstract

Ephrin receptors regulate intercellular communication and are thus involved in tumor development. Ephrin receptor A2 (EphA2), in particular, is overexpressed in a variety of cancers and is a proven target for anti-cancer drugs. The N-terminal ligand-binding domain of ephrin receptors is responsible for the recognition of their ligands, ephrins, and is directly involved in receptor activation. Here, we report on the complete ¹H, ¹⁵N and ¹³C NMR chemical shift assignment of EphA2 ligand binding domain that provides the basis for NMR-assisted drug design.

查看原文本刊更多论文

求助全文

约1分钟内获得全文求助全文

来源期刊

Biomolecular NMR Assignments 生物-光谱学

CiteScore

1.70

自引率

11.10%

发文量

审稿时长

6-12 weeks

期刊介绍： Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.