1xdt
From Proteopedia
(New page: 200px<br /> <applet load="1xdt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xdt, resolution 2.65Å" /> '''COMPLEX OF DIPHTHER...) |
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| - | [[Image:1xdt.gif|left|200px]]<br /> | + | [[Image:1xdt.gif|left|200px]]<br /><applet load="1xdt" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1xdt" size=" | + | |
caption="1xdt, resolution 2.65Å" /> | caption="1xdt, resolution 2.65Å" /> | ||
'''COMPLEX OF DIPHTHERIA TOXIN AND HEPARIN-BINDING EPIDERMAL GROWTH FACTOR'''<br /> | '''COMPLEX OF DIPHTHERIA TOXIN AND HEPARIN-BINDING EPIDERMAL GROWTH FACTOR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We describe the crystal structure at 2.65 A resolution of diphtheria toxin | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1XDT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/NAD(+)--diphthamide_ADP-ribosyltransferase NAD(+)--diphthamide ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.36 2.4.2.36] Full crystallographic information is available from [http:// | + | 1XDT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/NAD(+)--diphthamide_ADP-ribosyltransferase NAD(+)--diphthamide ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.36 2.4.2.36] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XDT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: NAD(+)--diphthamide ADP-ribosyltransferase]] | [[Category: NAD(+)--diphthamide ADP-ribosyltransferase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Bowman, M | + | [[Category: Bowman, M E.]] |
[[Category: Choe, S.]] | [[Category: Choe, S.]] | ||
| - | [[Category: Louie, G | + | [[Category: Louie, G V.]] |
[[Category: Yang, W.]] | [[Category: Yang, W.]] | ||
[[Category: complex (toxin/growth factor)]] | [[Category: complex (toxin/growth factor)]] | ||
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[[Category: receptor]] | [[Category: receptor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:53:42 2008'' |
Revision as of 13:53, 21 February 2008
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COMPLEX OF DIPHTHERIA TOXIN AND HEPARIN-BINDING EPIDERMAL GROWTH FACTOR
Contents |
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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