PDBsum entry 3lnd

Cell adhesion

PDB id

3lnd

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Contents

			Protein chains

					197 a.a. *


					202 a.a. *

			Metals

					_CA ×12

			Waters ×149

* Residue conservation analysis

PDB id:

3lnd

Links

Name:

Cell adhesion

Title:

Crystal structure of cadherin-6 ec12 w4a

Structure:

Cdh6 protein. Chain: a, b, c, d. Fragment: unp residues 54-260. Synonym: cadherin 6. Engineered: yes. Mutation: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: cdh6, mcg_8950. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.82Å

R-factor:

0.211

R-free:

0.282

Authors:

X.Jin,O.Harrison,L.Shapiro

Key ref:

O.J.Harrison et al. (2010). Two-step adhesive binding by classical cadherins. Nat Struct Biol, 17, 348-357. PubMed id: 20190754

Date:

02-Feb-10

Release date:

02-Mar-10

PROCHECK

	Headers

	References

Protein chain

P97326 (CADH6_MOUSE) - Cadherin-6 from Mus musculus

Seq: Struc:

Seq: Struc:					790 a.a. 197 a.a.

Protein chains

P97326 (CADH6_MOUSE) - Cadherin-6 from Mus musculus

Seq: Struc:

Seq: Struc:					790 a.a. 202 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)



		Enzyme reactions

Enzyme class:

Chains A, B, C, D: E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

	Nat Struct Biol 17:348-357 (2010)
PubMed id: 20190754

Two-step adhesive binding by classical cadherins.
O.J.Harrison, F.Bahna, P.S.Katsamba, X.Jin, J.Brasch, J.Vendome, G.Ahlsen, K.J.Carroll, S.R.Price, B.Honig, L.Shapiro.

ABSTRACT

Crystal structures of classical cadherins have revealed two dimeric configurations. In the first, N-terminal beta-strands of EC1 domains 'swap' between partner molecules. The second configuration (the 'X dimer'), also observed for T-cadherin, is mediated by residues near the EC1-EC2 calcium binding sites, and N-terminal beta-strands of partner EC1 domains, though held adjacent, do not swap. Here we show that strand-swapping mutants of type I and II classical cadherins form X dimers. Mutant cadherins impaired for X-dimer formation show no binding in short-time frame surface plasmon resonance assays, but in long-time frame experiments, they have homophilic binding affinities close to that of wild type. Further experiments show that exchange between monomers and dimers is slowed in these mutants. These results reconcile apparently disparate results from prior structural studies and suggest that X dimers are binding intermediates that facilitate the formation of strand-swapped dimers.

Literature references that cite this PDB file's key reference

PubMed id

Reference

21269602

J.Brasch, O.J.Harrison, G.Ahlsen, S.M.Carnally, R.M.Henderson, B.Honig, and L.Shapiro (2011).
Structure and binding mechanism of vascular endothelial cadherin: a divergent classical cadherin.

J Mol Biol, 408, 57-73.

PDB code:

3ppe

21572446

J.Vendome, S.Posy, X.Jin, F.Bahna, G.Ahlsen, L.Shapiro, and B.Honig (2011).
Molecular design principles underlying β-strand swapping in the adhesive dimerization of cadherins.

Nat Struct Mol Biol, 18, 693-700.

PDB code:

3qrb

21422232

S.Hong, R.B.Troyanovsky, and S.M.Troyanovsky (2011).
Cadherin exits the junction by switching its adhesive bond.

J Cell Biol, 192, 1073-1083.

20498078

H.M.Elledge, P.Kazmierczak, P.Clark, J.S.Joseph, A.Kolatkar, P.Kuhn, and U.Müller (2010).
Structure of the N terminus of cadherin 23 reveals a new adhesion mechanism for a subset of cadherin superfamily members.

Proc Natl Acad Sci U S A, 107, 10708-10712.

PDB code:

3mvs

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.