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<jats:p>A computational strategy to obtain structural insights into the poorly known interaction between EphA2 and the RNF5 proteins was set up<\/jats:p>\n                      <\/jats:list-item>\n                      <jats:list-item>\n                        <jats:label>\u2022<\/jats:label>\n                        <jats:p>\n                          <jats:italic toggle=\"yes\">In silico<\/jats:italic>\n                          studies suggest the RNF5 RING and TM2 domains as the best candidates for the interaction with EphA2-Sam\n                        <\/jats:p>\n                      <\/jats:list-item>\n                      <jats:list-item>\n                        <jats:label>\u2022<\/jats:label>\n                        <jats:p>Preliminary experimental validation with short synthetic peptides indicates that the RNF5 TM2 N-terminal side provides clear but unspecific weak binding<\/jats:p>\n                      <\/jats:list-item>\n                      <jats:list-item>\n                        <jats:label>\u2022<\/jats:label>\n                        <jats:p>RNF5 TM2 but not the TM1 domain assumes a perfect helical transmembrane structure topology according to computational resources<\/jats:p>\n                      <\/jats:list-item>\n                      <jats:list-item>\n                        <jats:label>\u2022<\/jats:label>\n                        <jats:p>The EphA2-Sam End Helix region is a \u201cuniversal\u201d binding site able to recruit multiple partners depending on the specific cancer cell context<\/jats:p>\n                      <\/jats:list-item>\n                    <\/jats:list>\n                  <\/jats:p>","DOI":"10.34133\/csbj.0166","type":"journal-article","created":{"date-parts":[[2026,6,23]],"date-time":"2026-06-23T22:42:18Z","timestamp":1782254538000},"update-policy":"https:\/\/doi.org\/10.34133\/aaas_crossmark_01","source":"Crossref","is-referenced-by-count":0,"title":["The Interaction between the Tyrosine Kinase Receptor EphA2 and 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