1xdt

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{{STRUCTURE_1xdt| PDB=1xdt | SCENE= }}
{{STRUCTURE_1xdt| PDB=1xdt | SCENE= }}
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'''COMPLEX OF DIPHTHERIA TOXIN AND HEPARIN-BINDING EPIDERMAL GROWTH FACTOR'''
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===COMPLEX OF DIPHTHERIA TOXIN AND HEPARIN-BINDING EPIDERMAL GROWTH FACTOR===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9659904 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9659904}}
==About this Structure==
==About this Structure==
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[[Category: Heparin-binding epidermal growth factor]]
[[Category: Heparin-binding epidermal growth factor]]
[[Category: Receptor]]
[[Category: Receptor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:53:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:22:26 2008''

Revision as of 18:22, 28 July 2008

Image:1xdt.png

Template:STRUCTURE 1xdt

COMPLEX OF DIPHTHERIA TOXIN AND HEPARIN-BINDING EPIDERMAL GROWTH FACTOR

Template:ABSTRACT PUBMED 9659904

About this Structure

1XDT is a Protein complex structure of sequences from Corynebacterium diphtheriae and Homo sapiens. 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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