Intrinsically disordered region of talin’s FERM domain functions as an initial PIP2 recognition site [research data]
<|begin_of_text|><|start_header_id|>system<|end_header_id|> You are a research archivist expert in dataset metadata. Answer the question truthfully.  <|eot_id|><|start_header_id|>user<|end_header_id|> Here is the Description of a dataset. Description:'Focal adhesions (FAs) mediate the interaction of the cytoskeleton with the extracellular matrix (ECM) in a highly dynamic fashion. talin is a central regulator, adaptor protein and mechano-sensor of focal adhesion complexes. For recruitment and firm attachment at FAs, talin’s N-terminal FERM domain binds to phosphatidylinositol 4,5-bisphosphate (PIP2)-enriched membranes. A newly published autoinhibitory structure of talin-1, where the known PIP2 interaction sites are covered up, lead us to hypothesize that a hitherto less examined loop insertion of the FERM domain acts as an additional and initial site of contact. We evaluated direct interactions of talin-1 with a PIP2 membrane by means of atomistic molecular dynamics (MD) simulations. We show that this unstructured, 33-residue-long loop strongly interact' . Please return only a json list of at most 3 Keywords corresponding to the Description:.<|eot_id|><|start_header_id|>assistant<|end_header_id|> {"Answer" : ["molecular dynamics","PIP2","talin-1"]} <|eot_id|>
 Here is the Description of a dataset. Description:'Focal adhesions (FAs) mediate the interaction of the cytoskeleton with the extracellular matrix (ECM) in a highly dynamic fashion. talin is a central regulator, adaptor protein and mechano-sensor of focal adhesion complexes. For recruitment and firm attachment at FAs, talin’s N-terminal FERM domain binds to phosphatidylinositol 4,5-bisphosphate (PIP2)-enriched membranes. A newly published autoinhibitory structure of talin-1, where the known PIP2 interaction sites are covered up, lead us to hypothesize that a hitherto less examined loop insertion of the FERM domain acts as an additional and initial site of contact. We evaluated direct interactions of talin-1 with a PIP2 membrane by means of atomistic molecular dynamics (MD) simulations. We show that this unstructured, 33-residue-long loop strongly interact' . Please return only a json list of at most 3 Keywords corresponding to the Description:.
Focal adhesions (FAs) mediate the interaction of the cytoskeleton with the extracellular matrix (ECM) in a highly dynamic fashion. talin is a central regulator, adaptor protein and mechano-sensor of focal adhesion complexes. For recruitment and firm attachment at FAs, talin’s N-terminal FERM domain binds to phosphatidylinositol 4,5-bisphosphate (PIP2)-enriched membranes. A newly published autoinhibitory structure of talin-1, where the known PIP2 interaction sites are covered up, lead us to hypothesize that a hitherto less examined loop insertion of the FERM domain acts as an additional and initial site of contact. We evaluated direct interactions of talin-1 with a PIP2 membrane by means of atomistic molecular dynamics (MD) simulations. We show that this unstructured, 33-residue-long loop strongly interact
molecular dynamics; PIP2; talin-1