PDBsum entry 3k5s

Structural protein

PDB id

3k5s

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Contents

			Protein chains

					217 a.a. *

			Metals

					_CA ×6

			Waters ×27

* Residue conservation analysis

PDB id:

3k5s

Links

Name:

Structural protein

Title:

Crystal structure of chicken t-cadherin ec1 ec2

Structure:

Cadherin-13. Chain: a, b. Fragment: domains ec1 and ec2 (unp residues 140 to 355). Synonym: truncated cadherin, t-cadherin, t-cad. Engineered: yes

Source:

Gallus gallus. Bantam,chickens. Organism_taxid: 9031. Gene: cdh13. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.90Å

R-factor:

0.213

R-free:

0.294

Authors:

L.Shapiro,C.Ciatto

Key ref:

C.Ciatto et al. (2010). T-cadherin structures reveal a novel adhesive binding mechanism. Nat Struct Biol, 17, 339-347. PubMed id: 20190755

Date:

07-Oct-09

Release date:

02-Mar-10

PROCHECK

	Headers

	References

Protein chains

P33150 (CAD13_CHICK) - Cadherin-13 from Gallus gallus

Seq: Struc:

Seq: Struc:					712 a.a. 217 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 2 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

E.C.?

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

	Nat Struct Biol 17:339-347 (2010)
PubMed id: 20190755

T-cadherin structures reveal a novel adhesive binding mechanism.
C.Ciatto, F.Bahna, N.Zampieri, H.C.VanSteenhouse, P.S.Katsamba, G.Ahlsen, O.J.Harrison, J.Brasch, X.Jin, S.Posy, J.Vendome, B.Ranscht, T.M.Jessell, B.Honig, L.Shapiro.

ABSTRACT

Vertebrate genomes encode 19 classical cadherins and about 100 nonclassical cadherins. Adhesion by classical cadherins depends on binding interactions in their N-terminal EC1 domains, which swap N-terminal beta-strands between partner molecules from apposing cells. However, strand-swapping sequence signatures are absent from nonclassical cadherins, raising the question of how these proteins function in adhesion. Here, we show that T-cadherin, a glycosylphosphatidylinositol (GPI)-anchored cadherin, forms dimers through an alternative nonswapped interface near the EC1-EC2 calcium-binding sites. Mutations within this interface ablate the adhesive capacity of T-cadherin. These nonadhesive T-cadherin mutants also lose the ability to regulate neurite outgrowth from T-cadherin-expressing neurons. Our findings reveal the likely molecular architecture of the T-cadherin homophilic interface and its requirement for axon outgrowth regulation. The adhesive binding mode used by T-cadherin may also be used by other nonclassical cadherins.

Literature references that cite this PDB file's key reference

PubMed id

Reference

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

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

21041950

M.S.Denzel, M.C.Scimia, P.M.Zumstein, K.Walsh, P.Ruiz-Lozano, and B.Ranscht (2010).
T-cadherin is critical for adiponectin-mediated cardioprotection in mice.

J Clin Invest, 120, 4342-4352.

20473317

S.Kjaer, S.Hanrahan, N.Totty, and N.Q.McDonald (2010).
Mammal-restricted elements predispose human RET to folding impairment by HSCR mutations.

Nat Struct Mol Biol, 17, 726-731.

PDB code:

2x2u

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.