Crystal structure of the TPR domain of KLC1 in complex with the C-terminal peptide of JIP1Crystal structure of the TPR domain of KLC1 in complex with the C-terminal peptide of JIP1

Structural highlights

6fuz is a 2 chain structure with sequence from Human and Lama. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:MAPK8IP1, IB1, JIP1, PRKM8IP (HUMAN)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Kinesin-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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Pernigo S, Lamprecht A, Steiner RA, Dodding MP. Structural Basis For Kinesin-1:Cargo Recognition. Science. 2013 Mar 21. PMID:23519214 doi:http://dx.doi.org/10.1126/science.1234264

6fuz, resolution 2.70Å

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