View source for 2v37


==Solution structure of the N-terminal extracellular domain of human T- cadherin==
<StructureSection load='2v37' size='340' side='right'caption='[[2v37]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2v37]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V37 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v37 OCA], [https://pdbe.org/2v37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v37 RCSB], [https://www.ebi.ac.uk/pdbsum/2v37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v37 ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/CAD13_HUMAN CAD13_HUMAN]] Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. May act as a negative regulator of neural cell growth.<ref>PMID:10737605</ref>  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v3/2v37_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2v37 ConSurf].
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== Publication Abstract from PubMed ==
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.

Insights into the low adhesive capacity of human T-cadherin from the NMR structure of Its N-terminal extracellular domain.,Dames SA, Bang E, Haussinger D, Ahrens T, Engel J, Grzesiek S J Biol Chem. 2008 Aug 22;283(34):23485-95. Epub 2008 Jun 10. PMID:18550521<ref>PMID:18550521</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Cadherin 3D structures|Cadherin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Ahrens, T]]
[[Category: Bang, E J]]
[[Category: Dames, S A]]
[[Category: Grzesiek, S]]
[[Category: Haeussinger, D]]
[[Category: Adiponectin receptor]]
[[Category: Calcium]]
[[Category: Cell adhesion]]
[[Category: Cell-cell adhesion]]
[[Category: Classical cadherin]]
[[Category: Cleavage on pair of basic residue]]
[[Category: Extracellular protein]]
[[Category: Glycoprotein]]
[[Category: Gpi-anchor]]
[[Category: Lipoprotein]]
[[Category: Membrane]]
[[Category: Polymorphism]]
[[Category: T-cadherin]]