1op4
From Proteopedia
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'''Solution Structure of Neural Cadherin Prodomain''' | '''Solution Structure of Neural Cadherin Prodomain''' | ||
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[[Category: Zeng, L.]] | [[Category: Zeng, L.]] | ||
[[Category: Zhou, M M.]] | [[Category: Zhou, M M.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:07:05 2008'' | |
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Revision as of 01:07, 3 May 2008
Solution Structure of Neural Cadherin Prodomain
Overview
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.
About this Structure
1OP4 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of the neural (N-) cadherin prodomain reveals a cadherin extracellular domain-like fold without adhesive characteristics., Koch AW, Farooq A, Shan W, Zeng L, Colman DR, Zhou MM, Structure. 2004 May;12(5):793-805. PMID:15130472 Page seeded by OCA on Sat May 3 04:07:05 2008
