1cs6

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(New page: 200px<br /><applet load="1cs6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cs6, resolution 1.80&Aring;" /> '''N-TERMINAL FRAGMENT ...)
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[[Image:1cs6.gif|left|200px]]<br /><applet load="1cs6" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1cs6.gif|left|200px]]<br /><applet load="1cs6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1cs6, resolution 1.80&Aring;" />
caption="1cs6, resolution 1.80&Aring;" />
'''N-TERMINAL FRAGMENT OF AXONIN-1 FROM CHICKEN'''<br />
'''N-TERMINAL FRAGMENT OF AXONIN-1 FROM CHICKEN'''<br />
==Overview==
==Overview==
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We have determined the crystal structure of the ligand binding fragment of, the neural cell adhesion molecule axonin-1/TAG-1 comprising the first four, immunoglobulin (Ig) domains. The overall structure of axonin-1(Ig1-4) is, U-shaped due to contacts between domains 1 and 4 and domains 2 and 3. In, the crystals, these molecules are aligned in a string with adjacent, molecules oriented in an anti-parallel fashion and their C termini, perpendicular to the string. This arrangement suggests that cell adhesion, by homophilic axonin-1 interaction occurs by the formation of a linear, zipper-like array in which the axonin-1 molecules are alternately provided, by the two apposed membranes. In accordance with this model, mutations in, a loop critical for the formation of the zipper resulted in the loss of, the homophilic binding capacity of axonin-1.
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We have determined the crystal structure of the ligand binding fragment of the neural cell adhesion molecule axonin-1/TAG-1 comprising the first four immunoglobulin (Ig) domains. The overall structure of axonin-1(Ig1-4) is U-shaped due to contacts between domains 1 and 4 and domains 2 and 3. In the crystals, these molecules are aligned in a string with adjacent molecules oriented in an anti-parallel fashion and their C termini perpendicular to the string. This arrangement suggests that cell adhesion by homophilic axonin-1 interaction occurs by the formation of a linear zipper-like array in which the axonin-1 molecules are alternately provided by the two apposed membranes. In accordance with this model, mutations in a loop critical for the formation of the zipper resulted in the loss of the homophilic binding capacity of axonin-1.
==About this Structure==
==About this Structure==
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1CS6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CS6 OCA].
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1CS6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CS6 OCA].
==Reference==
==Reference==
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[[Category: neural cell adhesion]]
[[Category: neural cell adhesion]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:43:10 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:09:12 2008''

Revision as of 10:09, 21 February 2008


1cs6, resolution 1.80Å

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N-TERMINAL FRAGMENT OF AXONIN-1 FROM CHICKEN

Overview

We have determined the crystal structure of the ligand binding fragment of the neural cell adhesion molecule axonin-1/TAG-1 comprising the first four immunoglobulin (Ig) domains. The overall structure of axonin-1(Ig1-4) is U-shaped due to contacts between domains 1 and 4 and domains 2 and 3. In the crystals, these molecules are aligned in a string with adjacent molecules oriented in an anti-parallel fashion and their C termini perpendicular to the string. This arrangement suggests that cell adhesion by homophilic axonin-1 interaction occurs by the formation of a linear zipper-like array in which the axonin-1 molecules are alternately provided by the two apposed membranes. In accordance with this model, mutations in a loop critical for the formation of the zipper resulted in the loss of the homophilic binding capacity of axonin-1.

About this Structure

1CS6 is a Single protein structure of sequence from Gallus gallus with as ligand. Full crystallographic information is available from OCA.

Reference

The crystal structure of the ligand binding module of axonin-1/TAG-1 suggests a zipper mechanism for neural cell adhesion., Freigang J, Proba K, Leder L, Diederichs K, Sonderegger P, Welte W, Cell. 2000 May 12;101(4):425-33. PMID:10830169

Page seeded by OCA on Thu Feb 21 12:09:12 2008

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