1OP4

Solution Structure of Neural Cadherin Prodomain

Summary for 1OP4

• Entry DOI: 10.2210/pdb1op4/pdb
• NMR Information: BMRB: 5786
• Descriptor: Neural-cadherin (1 entity in total)
• Functional Keywords: beta sandwich, cadherin-like domain, cell adhesion
• Biological source: Mus musculus (house mouse)
• Cellular location: Cell membrane; Single-pass type I membrane protein: P15116
• Total number of polymer chains: 1
• Total formula weight: 18336.39

Authors

Koch, A.W.,Farooq, A.,Shan, W.,Zeng, L.,Colman, D.R.,Zhou, M.-M. (deposition date: 2003-03-04, release date: 2004-03-16, Last modification date: 2024-11-06)

Primary citation

Koch, A.W.,Farooq, A.,Shan, W.,Zeng, L.,Colman, D.R.,Zhou, M.-M.
Structure of the Neural (N-) Cadherin Prodomain Reveals a Cadherin Extracellular Domain-like Fold without Adhesive Characteristics
Structure, 12:793-805, 2004

PubMed Abstract: Classical cadherins mediate cell-cell adhesion through calcium-dependent homophilic interactions and are activated through cleavage of a prosequence in the late Golgi. We present here the first three-dimensional structure of a classical cadherin prosequence, solved by NMR. The prototypic prosequence of N-cadherin consists of an Ig-like domain and an unstructured C-terminal region. The folded part of the prosequence-termed prodomain-has a striking structural resemblance to cadherin "adhesive" domains that could not have been predicted from the amino acid sequence due to low sequence similarities. Our detailed structural and evolutionary analysis revealed that prodomains are distant relatives of cadherin "adhesive" domains but lack all the features known to be important for cadherin-cadherin interactions. The presence of an additional "nonadhesive" domain seems to make it impossible to engage homophilic interactions between cadherins that are necessary to activate adhesion, thus explaining the inactive state of prodomain-bearing cadherins.

PubMed: 15130472
DOI: 10.1016/j.str.2004.02.034

Experimental method

SOLUTION NMR