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2WD0

CRYSTAL STRUCTURE OF NONSYNDROMIC DEAFNESS (DFNB12) ASSOCIATED MUTANT D124G OF MOUSE CADHERIN-23 EC1-2

Summary for 2WD0
Entry DOI10.2210/pdb2wd0/pdb
Related2WBX 2WCP
DescriptorCADHERIN-23, CALCIUM ION, SODIUM ION, ... (5 entities in total)
Functional Keywordscell adhesion, hearing
Biological sourceMUS MUSCULUS (HOUSE MOUSE)
Cellular locationCell membrane; Single-pass type I membrane protein (By similarity): Q99PF4
Total number of polymer chains2
Total formula weight47989.61
Authors
Sotomayor, M.,Weihofen, W.,Gaudet, R.,Corey, D.P. (deposition date: 2009-03-18, release date: 2010-04-21, Last modification date: 2023-12-13)
Primary citationSotomayor, M.,Weihofen, W.,Gaudet, R.,Corey, D.P.
Structural Determinants of Cadherin-23 Function in Hearing and Deafness.
Neuron, 66:85-, 2010
Cited by
PubMed Abstract: The hair-cell tip link, a fine filament directly conveying force to mechanosensitive transduction channels, is composed of two proteins, protocadherin-15 and cadherin-23, whose mutation causes deafness. However, their molecular structure, elasticity, and deafness-related structural defects are unknown. We present crystal structures of the first and second extracellular cadherin repeats of cadherin-23. Overall, structures show typical cadherin folds, but reveal an elongated N terminus that precludes classical cadherin interactions and contributes to an N-terminal Ca(2+)-binding site. The deafness mutation D101G, in the linker region between the repeats, causes a slight bend between repeats and decreases Ca(2+) affinity. Molecular dynamics simulations suggest that cadherin-23 repeats are stiff and that either removing Ca(2+) or mutating Ca(2+)-binding residues reduces rigidity and unfolding strength. The structures define an uncharacterized cadherin family and, with simulations, suggest mechanisms underlying inherited deafness and how cadherin-23 may bind with itself and with protocadherin-15 to form the tip link.
PubMed: 20399731
DOI: 10.1016/J.NEURON.2010.03.028
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.74 Å)
Structure validation

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