Cadherins are a family of proteins that mediate calcium dependent cell-cell adhesion. They are activated through cleavage of a prosequence in the late Golgi. This domain corresponds to the folded region of the prosequence, and is termed the prodomain. The prodomain shows structural resemblance to the cadherin domain, but lacks all the features known to be important for cadherin-cadherin interactions (PUBMED:15130472).
Cadherins are a group of proteins that mediate calcium dependent cell-cell adhesion. They are activated through cleavage of a prosequence in the late Golgi. The folded part of the prosequence (termed the prodomain) shows structural resemblance to cadherin adhesive domains, but lacks all the features known to be important for cadherin-cadherin interactions [ (PUBMED:15130472) ].
This entry represents the caderin prodomain.
Family alignment:
There are 1917 Cadherin_pro domains in 1912 proteins in SMART's nrdb database.
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Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing Cadherin_pro domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with Cadherin_pro domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing Cadherin_pro domain in the selected taxonomic class.
Structure of the neural (N-) cadherin prodomain reveals a cadherinextracellular domain-like fold without adhesive characteristics.
Structure. 2004; 12: 793-805
Display abstract
Classical cadherins mediate cell-cell adhesion through calcium-dependenthomophilic interactions and are activated through cleavage of aprosequence in the late Golgi. We present here the first three-dimensionalstructure of a classical cadherin prosequence, solved by NMR. Theprototypic prosequence of N-cadherin consists of an Ig-like domain and anunstructured C-terminal region. The folded part of the prosequence-termedprodomain-has a striking structural resemblance to cadherin "adhesive"domains that could not have been predicted from the amino acid sequencedue to low sequence similarities. Our detailed structural and evolutionaryanalysis revealed that prodomains are distant relatives of cadherin"adhesive" domains but lack all the features known to be important forcadherin-cadherin interactions. The presence of an additional"nonadhesive" domain seems to make it impossible to engage homophilicinteractions between cadherins that are necessary to activate adhesion,thus explaining the inactive state of prodomain-bearing cadherins.
S-S-lambda-shaped TRANS and CIS interactions of cadherins model based on fitting C-cadherin (1L3W) to 3D map of desmosomes obtained by electron tomography
Links (links to other resources describing this domain)
