http://purl.uniprot.org/citations/33838110 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/33838110 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/33838110 | http://www.w3.org/2000/01/rdf-schema#comment | "Synthetic peptides are attractive candidates to manipulate protein-protein interactions inside the cell as they mimic natural interactions to compete for binding. However, protein-peptide interactions are often dynamic and weak. A challenge is to design peptides that make improved interactions with the target. Here, we devise a fragment-linking strategy-"mash-up" design-to deliver a high-affinity ligand, KinTag, for the kinesin-1 motor. Using structural insights from natural micromolar-affinity cargo-adaptor ligands, we have identified and combined key binding features in a single, high-affinity ligand. An X-ray crystal structure demonstrates interactions as designed and reveals only a modest increase in interface area. Moreover, when genetically encoded, KinTag promotes transport of lysosomes with higher efficiency than natural sequences, revealing a direct link between motor-adaptor binding affinity and organelle transport. Together, these data demonstrate a fragment-linking strategy for peptide design and its application in a synthetic motor ligand to direct cellular cargo transport."xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.chembiol.2021.03.010"xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.chembiol.2021.03.010"xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/author | "Woolfson D.N."xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/author | "Woolfson D.N."xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/author | "Dodding M.P."xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/author | "Dodding M.P."xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/author | "Cross J.A."xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/author | "Cross J.A."xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/author | "Steiner R.A."xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/author | "Steiner R.A."xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/author | "Chegkazi M.S."xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/author | "Chegkazi M.S."xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/name | "Cell Chem. Biol."xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/name | "Cell Chem Biol"xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/pages | "1347-1355.e5"xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/pages | "1347-1355.e5"xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/title | "Fragment-linking peptide design yields a high-affinity ligand for microtubule-based transport."xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/title | "Fragment-linking peptide design yields a high-affinity ligand for microtubule-based transport."xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/volume | "28"xsd:string |
http://purl.uniprot.org/citations/33838110 | http://purl.uniprot.org/core/volume | "28"xsd:string |