3LAF

Structure of DCC, a netrin-1 receptor

Summary for 3LAF

• Entry DOI: 10.2210/pdb3laf/pdb
• Descriptor: Deleted in Colorectal Cancer, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: netrin-1 receptor, immunoglobulin superfamily, horseshoe, apoptosis
• Biological source: Rattus norvegicus (rat)
• Cellular location: Membrane ; Single-pass type I membrane protein : Q63155
• Total number of polymer chains: 1
• Total formula weight: 46900.99

Authors

Chen, Q.,Liu, J.-H.,Wang, J.-H. (deposition date: 2010-01-06, release date: 2011-03-02, Last modification date: 2024-10-30)

Primary citation

Chen, Q.,Sun, X.,Zhou, X.H.,Liu, J.H.,Wu, J.,Zhang, Y.,Wang, J.H.
N-terminal horseshoe conformation of DCC is functionally required for axon guidance and might be shared by other neural receptors.
J.Cell.Sci., 126:186-195, 2013

PubMed Abstract: Deleted in colorectal cancer (DCC) is a receptor for the axon guidance cues netrin-1 and draxin. The interactions between these guidance cues and DCC play a key role in the development of the nervous system. In the present study, we reveal the crystal structure of the N-terminal four Ig-like domains of DCC. The molecule folds into a horseshoe-like configuration. We demonstrate that this horseshoe conformation of DCC is required for guidance-cue-mediated axonal attraction. Structure-based mutations that disrupt the DCC horseshoe indeed impair its function. A comparison of the DCC horseshoe with previously described horseshoe structures has revealed striking conserved structural features and important sequence signatures. Using these signatures, a genome-wide search allows us to predict the N-terminal horseshoe arrangement in a number of other cell surface receptors, nearly all of which function in the nervous system. The N-terminal horseshoe appears to be evolutionally selected as a platform for neural receptors.

PubMed: 23038776
DOI: 10.1242/jcs.111278

Experimental method

X-RAY DIFFRACTION (2.4 Å)