This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3ppe

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Crystal structure of chicken VE-cadherin EC1-2

Structural highlights

3ppe is a 2 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CADH5_CHICK 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. This cadherin may play a important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions.^[1]

Publication Abstract from PubMed

Vascular endothelial cadherin (VE-cadherin), a divergent member of the type II classical cadherin family of cell adhesion proteins, mediates homophilic adhesion in the vascular endothelium. Previous investigations with a bacterially produced protein suggested that VE-cadherin forms cell surface trimers that bind between apposed cells to form hexamers. Here we report studies of mammalian-produced VE-cadherin ectodomains suggesting that, like other classical cadherins, VE-cadherin forms adhesive trans dimers between monomers located on opposing cell surfaces. Trimerization of the bacterially produced protein appears to be an artifact that arises from a lack of glycosylation. We also present the 2.1-A-resolution crystal structure of the VE-cadherin EC1-2 adhesive region, which reveals homodimerization via the strand-swap mechanism common to classical cadherins. In common with type II cadherins, strand-swap binding involves two tryptophan anchor residues, but the adhesive interface resembles type I cadherins in that VE-cadherin does not form a large nonswapped hydrophobic surface. Thus, VE-cadherin is an outlier among classical cadherins, with characteristics of both type I and type II subfamilies.

Structure and binding mechanism of vascular endothelial cadherin: a divergent classical cadherin.,Brasch J, Harrison OJ, Ahlsen G, Carnally SM, Henderson RM, Honig B, Shapiro L J Mol Biol. 2011 Apr 22;408(1):57-73. Epub 2011 Jan 24. PMID:21269602^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Brasch J, Harrison OJ, Ahlsen G, Carnally SM, Henderson RM, Honig B, Shapiro L. Structure and binding mechanism of vascular endothelial cadherin: a divergent classical cadherin. J Mol Biol. 2011 Apr 22;408(1):57-73. Epub 2011 Jan 24. PMID:21269602 doi:10.1016/j.jmb.2011.01.031
↑ Brasch J, Harrison OJ, Ahlsen G, Carnally SM, Henderson RM, Honig B, Shapiro L. Structure and binding mechanism of vascular endothelial cadherin: a divergent classical cadherin. J Mol Biol. 2011 Apr 22;408(1):57-73. Epub 2011 Jan 24. PMID:21269602 doi:10.1016/j.jmb.2011.01.031

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ppe"

@@ Line 1: / Line 1: @@
 ==Crystal structure of chicken VE-cadherin EC1-2==
-<StructureSection load='3ppe' size='340' side='right' caption='[[3ppe]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='3ppe' size='340' side='right'caption='[[3ppe]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3ppe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PPE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PPE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3ppe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PPE FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ppe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ppe RCSB], [http://www.ebi.ac.uk/pdbsum/3ppe PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=3ppe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppe OCA], [https://pdbe.org/3ppe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ppe RCSB], [https://www.ebi.ac.uk/pdbsum/3ppe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ppe ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/CADH5_CHICK CADH5_CHICK] 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. This cadherin may play a important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions.<ref>PMID:21269602</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 14: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3ppe" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Cadherin|Cadherin]]
+*[[Cadherin 3D structures|Cadherin 3D structures]]
 == References ==
 <references/>
@@ Line 22: / Line 27: @@
 </StructureSection>
 [[Category: Gallus gallus]]
-[[Category: Ahlsen, G]]
+[[Category: Large Structures]]
-[[Category: Brasch, J]]
+[[Category: Ahlsen G]]
-[[Category: Carnally, S M]]
+[[Category: Brasch J]]
-[[Category: Harrison, O J]]
+[[Category: Carnally SM]]
-[[Category: Henderson, R M]]
+[[Category: Harrison OJ]]
-[[Category: Honig, B]]
+[[Category: Henderson RM]]
-[[Category: Shapiro, L S]]
+[[Category: Honig B]]
-[[Category: Beta barrel]]
+[[Category: Shapiro LS]]
-[[Category: Calcium dependent cell-cell adhesion]]
-[[Category: Cell adhesion]]
-[[Category: Cell surface]]
-[[Category: Domain swapped dimer interface]]
-[[Category: Ig-domain like]]

3ppe

From Proteopedia

Current revision

Crystal structure of chicken VE-cadherin EC1-2

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox