Abstract
Crystal Structures of the Single PDZ Domains from GRASP65 and their Interaction with the Golgin GM130
Highlights
A S part of the endomembrane system of eukaryotic cells, the Golgi apparatus is traversed by proteins originating from the endoplasmic reticulum (ER) as they translocate to their final destination in or beyond the plasma membrane
The second PDZ domain, GRASP65PDZ2, was crystallized (Figure 1C) and exhibited the typical PDZ fold consisting of five β-strands and two α-helices
We present the crystal structures of the two separate PDZ domains of human GRASP65, GRASP65PDZ1 and GRASP65PDZ2
Summary
A S part of the endomembrane system of eukaryotic cells, the Golgi apparatus is traversed by proteins originating from the endoplasmic reticulum (ER) as they translocate to their final destination in or beyond the plasma membrane. It is composed of cisternal membrane structures arranged in Golgi stacks which are further organized into a larger ribbon structure.[1] The Golgi apparatus has three primary compartments, known as “cis” (cisternae nearest the endoplasmic reticulum), “medial” (central layers of cisternae), and “trans” (cisternae farthest from the endoplasmic reticulum). Interaction with the C-terminus of the Golgi marker protein GM130 recruits GRASP65 to the cis-Golgi membrane where it is involved in the docking of transport vesicles to the Golgi membrane.[5,7,8]
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