6swu

Crystal structure of the TPR domain of KLC1 in complex with an engineered high-affinity cargo peptide.

spinqualitylabelsall models 6swu, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6swu is a 6 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.849Å Ligands: EDO, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5UE59_MOUSE Publication Abstract from PubMed 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. Fragment-linking peptide design yields a high-affinity ligand for microtubule-based transport.,Cross JA, Chegkazi MS, Steiner RA, Woolfson DN, Dodding MP Cell Chem Biol. 2021 Mar 31. pii: S2451-9456(21)00149-5. doi:, 10.1016/j.chembiol.2021.03.010. PMID:33838110 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Kinesin 3D Structures

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