1rj8

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(New page: 200px<br /> <applet load="1rj8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rj8, resolution 2.23&Aring;" /> '''The crystal structu...)
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[[Image:1rj8.gif|left|200px]]<br />
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[[Image:1rj8.gif|left|200px]]<br /><applet load="1rj8" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1rj8" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1rj8, resolution 2.23&Aring;" />
caption="1rj8, resolution 2.23&Aring;" />
'''The crystal structure of TNF family member EDA-A2'''<br />
'''The crystal structure of TNF family member EDA-A2'''<br />
==Overview==
==Overview==
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EDA is a tumor necrosis factor family member involved in ectodermal, development. Splice variants EDA-A1 and EDA-A2 differ only by the presence, of Glu 308 and Val 309 in the expected receptor binding region of EDA-A1, but not EDA-A2. This two amino acid difference functions as a switch, controlling receptor specificity. EDA-A1 binds only to EDAR, while EDA-A2, is specific for XEDAR. In order to understand the structural basis of this, switch, we determined the X-ray crystal structures of the TNF domain of, both EDA-A1 and EDA-A2 at 2.3 A and 2.2 A, respectively. While the, backbone conformation around the splice difference is similar in both, isoforms, the conformation of the following loop, the surface charge, and, the shape of the expected receptor binding site differ significantly.
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EDA is a tumor necrosis factor family member involved in ectodermal development. Splice variants EDA-A1 and EDA-A2 differ only by the presence of Glu 308 and Val 309 in the expected receptor binding region of EDA-A1 but not EDA-A2. This two amino acid difference functions as a switch controlling receptor specificity. EDA-A1 binds only to EDAR, while EDA-A2 is specific for XEDAR. In order to understand the structural basis of this switch, we determined the X-ray crystal structures of the TNF domain of both EDA-A1 and EDA-A2 at 2.3 A and 2.2 A, respectively. While the backbone conformation around the splice difference is similar in both isoforms, the conformation of the following loop, the surface charge, and the shape of the expected receptor binding site differ significantly.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1RJ8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RJ8 OCA].
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1RJ8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RJ8 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ackerly, H.]]
[[Category: Ackerly, H.]]
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[[Category: Compaan, D.M.]]
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[[Category: Compaan, D M.]]
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[[Category: Dixit, V.M.]]
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[[Category: Dixit, V M.]]
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[[Category: Hymowitz, S.G.]]
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[[Category: Hymowitz, S G.]]
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[[Category: Starovasnik, M.A.]]
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[[Category: Starovasnik, M A.]]
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[[Category: Vos, A.M.de.]]
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[[Category: Vos, A M.de.]]
[[Category: Yan, M.]]
[[Category: Yan, M.]]
[[Category: jelly roll]]
[[Category: jelly roll]]
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[[Category: trimer]]
[[Category: trimer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:04:23 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:39 2008''

Revision as of 12:51, 21 February 2008


1rj8, resolution 2.23Å

Drag the structure with the mouse to rotate

The crystal structure of TNF family member EDA-A2

Contents

Overview

EDA is a tumor necrosis factor family member involved in ectodermal development. Splice variants EDA-A1 and EDA-A2 differ only by the presence of Glu 308 and Val 309 in the expected receptor binding region of EDA-A1 but not EDA-A2. This two amino acid difference functions as a switch controlling receptor specificity. EDA-A1 binds only to EDAR, while EDA-A2 is specific for XEDAR. In order to understand the structural basis of this switch, we determined the X-ray crystal structures of the TNF domain of both EDA-A1 and EDA-A2 at 2.3 A and 2.2 A, respectively. While the backbone conformation around the splice difference is similar in both isoforms, the conformation of the following loop, the surface charge, and the shape of the expected receptor binding site differ significantly.

Disease

Known diseases associated with this structure: Ectodermal dysplasia-1, anhidrotic OMIM:[300451], Hypodontia, X-linked OMIM:[300451]

About this Structure

1RJ8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The crystal structures of EDA-A1 and EDA-A2: splice variants with distinct receptor specificity., Hymowitz SG, Compaan DM, Yan M, Wallweber HJ, Dixit VM, Starovasnik MA, de Vos AM, Structure. 2003 Dec;11(12):1513-20. PMID:14656435

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