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1xdt
From Proteopedia
COMPLEX OF DIPHTHERIA TOXIN AND HEPARIN-BINDING EPIDERMAL GROWTH FACTOR
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1XDT is a 2 chains structure of sequences from Corynebacterium diphtheriae and Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Louie GV, Yang W, Bowman ME, Choe S. Crystal structure of the complex of diphtheria toxin with an extracellular fragment of its receptor. Mol Cell. 1997 Dec;1(1):67-78. PMID:9659904
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