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 1.80Å" /> '''N-TERMINAL FRAGMENT ...)
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Revision as of 10:35, 20 November 2007
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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 GOL 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 Tue Nov 20 12:43:10 2007
