1cs6

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|ACTIVITY=
|ACTIVITY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cs6 OCA], [http://www.ebi.ac.uk/pdbsum/1cs6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cs6 RCSB]</span>
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[[Category: Sonderegger, P.]]
[[Category: Sonderegger, P.]]
[[Category: Welte, W.]]
[[Category: Welte, W.]]
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[[Category: GOL]]
 
[[Category: neural cell adhesion]]
[[Category: neural cell adhesion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:28:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:27:32 2008''

Revision as of 16:27, 30 March 2008


PDB ID 1cs6

Drag the structure with the mouse to rotate
, resolution 1.80Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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