1CS6

N-TERMINAL FRAGMENT OF AXONIN-1 FROM CHICKEN

Summary for 1CS6

• Entry DOI: 10.2210/pdb1cs6/pdb
• Descriptor: AXONIN-1, GLYCEROL (3 entities in total)
• Functional Keywords: neural cell adhesion, cell adhesion
• Biological source: Gallus gallus (chicken)
• Cellular location: Cell membrane; Lipid-anchor, GPI-anchor: P28685
• Total number of polymer chains: 1
• Total formula weight: 42694.83

Authors

Freigang, J.,Proba, K.,Diederichs, K.,Sonderegger, P.,Welte, W. (deposition date: 1999-08-17, release date: 2000-05-19, Last modification date: 2024-10-30)

Primary citation

Freigang, J.,Proba, K.,Leder, L.,Diederichs, K.,Sonderegger, P.,Welte, W.
The crystal structure of the ligand binding module of axonin-1/TAG-1 suggests a zipper mechanism for neural cell adhesion.
Cell(Cambridge,Mass.), 101:425-433, 2000

PubMed Abstract: 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.

PubMed: 10830169
DOI: 10.1016/S0092-8674(00)80852-1

Experimental method

X-RAY DIFFRACTION (1.8 Å)