1cs6

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[[Image:1cs6.gif|left|200px]]
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{{STRUCTURE_1cs6| PDB=1cs6 | SCENE= }}
{{STRUCTURE_1cs6| PDB=1cs6 | SCENE= }}
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'''N-TERMINAL FRAGMENT OF AXONIN-1 FROM CHICKEN'''
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===N-TERMINAL FRAGMENT OF AXONIN-1 FROM CHICKEN===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 10830169 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10830169}}
==About this Structure==
==About this Structure==
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[[Category: Welte, W.]]
[[Category: Welte, W.]]
[[Category: Neural cell adhesion]]
[[Category: Neural cell adhesion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:03:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:15:52 2008''

Revision as of 18:15, 30 June 2008

Image:1cs6.png

Template:STRUCTURE 1cs6

N-TERMINAL FRAGMENT OF AXONIN-1 FROM CHICKEN

Template:ABSTRACT PUBMED 10830169

About this Structure

1CS6 is a Single protein structure of sequence from Gallus gallus. 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

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