1xdt

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spinqualitylabelsall models 1xdt, resolution 2.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

COMPLEX OF DIPHTHERIA TOXIN AND HEPARIN-BINDING EPIDERMAL GROWTH FACTOR

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

We describe the crystal structure at 2.65 A resolution of diphtheria toxin, (DT) complexed 1:1 with a fragment of its cell-surface receptor, the, precursor of heparin-binding epidermal-growth-factor-like growth factor, (HBEGF). HBEGF in the complex has the typical EGF-like fold and packs its, principal beta hairpin against the face of a beta sheet in the, receptor-binding domain of DT. The interface has a predominantly, hydrophobic core, and polar interactions are formed at the periphery. The, structure of the complex suggests that part of the membrane anchor of the, receptor can interact with a hinge region of DT. The toxin molecule is, thereby induced to form an open conformation conducive to membrane, insertion. The structure provides a basis for altering the binding, specificity of the toxin, and may also serve as a model for other, EGF-receptor interactions.

Disease

Known diseases associated with this structure: Diphtheria, susceptibility to OMIM:[126150]

About this Structure

1XDT is a Protein complex structure of sequences from Corynebacterium diphtheriae and Homo sapiens. Active as NAD(+)--diphthamide ADP-ribosyltransferase, with EC number 2.4.2.36 Full crystallographic information is available from OCA.

Reference

Crystal structure of the complex of diphtheria toxin with an extracellular fragment of its receptor., Louie GV, Yang W, Bowman ME, Choe S, Mol Cell. 1997 Dec;1(1):67-78. PMID:9659904

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