2V37

Solution structure of the N-terminal extracellular domain of human T- cadherin


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 20 
  • Selection Criteria: LOWEST ENERGY 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Insights into the low adhesive capacity of human T-cadherin from the NMR structure of Its N-terminal extracellular domain.

Dames, S.A.Bang, E.Haussinger, D.Ahrens, T.Engel, J.Grzesiek, S.

(2008) J Biol Chem 283: 23485-23495

  • DOI: https://doi.org/10.1074/jbc.M708335200
  • Primary Citation of Related Structures:  
    2V37

  • PubMed Abstract: 

    T-cadherin is unique among the family of type I cadherins, because it lacks transmembrane and cytosolic domains, and attaches to the membrane via a glycophosphoinositol anchor. The N-terminal cadherin repeat of T-cadherin (Tcad1) is approximately 30% identical to E-, N-, and other classical cadherins. However, it lacks many amino acids crucial for their adhesive function of classical cadherins. Among others, Trp-2, which is the key residue forming the canonical strand-exchange dimer, is replaced by an isoleucine. Here, we report the NMR structure of the first cadherin repeat of T-cadherin (Tcad1). Tcad1, as other cadherin domains, adopts a beta-barrel structure with a Greek key folding topology. However, Tcad1 is monomeric in the absence and presence of calcium. Accordingly, lle-2 binds into a hydrophobic pocket on the same protomer and participates in an N-terminal beta-sheet. Specific amino acid replacements compared to classical cadherins reduce the size of the binding pocket for residue 2 and alter the backbone conformation and flexibility around residues 5 and 15 as well as many electrostatic interactions. These modifications apparently stabilize the monomeric form and make it less susceptible to a conformational switch upon calcium binding. The absence of a tendency for homoassociation observed by NMR is consistent with electron microscopy and solid-phase binding data of the full T-cadherin ectodomain (Tcad1-5). The apparent low adhesiveness of T-cadherin suggests that it is likely to be involved in reversible and dynamic cellular adhesion-deadhesion processes, which are consistent with its role in cell growth and migration.


  • Organizational Affiliation

    Department of Structural Biology, University of Basel, Klingelbergstr. 70, 4056 Basel, Switzerland. sonja.dames@unibas.ch


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CADHERIN-13105Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P55290 (Homo sapiens)
Explore P55290 
Go to UniProtKB:  P55290
PHAROS:  P55290
GTEx:  ENSG00000140945 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP55290
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 20 
  • Selection Criteria: LOWEST ENERGY 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-06-10
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-03-28
    Changes: Data collection, Database references, Source and taxonomy
  • Version 1.4: 2024-05-15
    Changes: Data collection, Database references, Other