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1cs6
From Proteopedia
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[[Image:1cs6.gif|left|200px]] | [[Image:1cs6.gif|left|200px]] | ||
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'''N-TERMINAL FRAGMENT OF AXONIN-1 FROM CHICKEN''' | '''N-TERMINAL FRAGMENT OF AXONIN-1 FROM CHICKEN''' | ||
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[[Category: Sonderegger, P.]] | [[Category: Sonderegger, P.]] | ||
[[Category: Welte, W.]] | [[Category: Welte, W.]] | ||
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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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Revision as of 10:03, 2 May 2008
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. 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 Fri May 2 13:03:39 2008
