3zfw | pdb_00003zfw
From Proteopedia
Crystal structure of the TPR domain of kinesin light chain 2 in complex with a tryptophan-acidic cargo peptide
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Structural highlights
Function[PKHM2_HUMAN] May play a role in the regulation of conventional kinesin activity. Required for maintenance of the Golgi apparatus organization. May play a role in membrane tubulation.[1] Publication Abstract from PubMedKinesin-mediated cargo transport is required for many cellular functions and plays a key role in pathological processes. Structural information on how kinesins recognize their cargoes is required for a molecular understanding of this fundamental and ubiquitous process. Here, we present the crystal structure of the tetratricopeptide repeat of kinesin light chain 2 in complex with a cargo peptide harboring a 'tryptophan-acidic' motif derived from SKIP, a critical host determinant in Salmonella pathogenesis and a regulator of lysosomal positioning. Structural data together with biophysical, biochemical, and cellular assays allow us to propose a framework for intracellular transport based on the binding by kinesin-1 of W-acidic cargo motifs through a combination of electrostatic interactions and sequence-specific elements, providing direct molecular evidence of the mechanisms for kinesin-1:cargo recognition. Structural Basis For Kinesin-1:Cargo Recognition.,Pernigo S, Lamprecht A, Steiner RA, Dodding MP Science. 2013 Mar 21. PMID:23519214[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 05:45, 10 August 2022.