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PDBsum entry 1q1p
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protein metals links
Cell adhesion PDB id
1q1p

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
212 a.a. *
Metals
_CA ×3
Waters ×233
* Residue conservation analysis
PDB id:
1q1p
Name: Cell adhesion
Title: E-cadherin activation
Structure: Epithelial-cadherin. Chain: a. Synonym: e-cadherin, uvomorulin, cadherin-1, arc-1. Engineered: yes
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: cdh1. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
3.20Å     R-factor:   0.262     R-free:   0.305
Authors: D.Haussinger,J.Stetefeld
Key ref:
D.Häussinger et al. (2004). Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography. EMBO J, 23, 1699-1708. PubMed id: 15071499 DOI: 10.1038/sj.emboj.7600192
Date:
22-Jul-03     Release date:   20-Apr-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P09803  (CADH1_MOUSE) -  Cadherin-1 from Mus musculus
Seq:
Struc: 		 
Seq:
Struc: 		884 a.a.
212 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1038/sj.emboj.7600192 EMBO J 23:1699-1708 (2004)
PubMed id: 15071499  
 
 
Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography.
D.Häussinger, T.Ahrens, T.Aberle, J.Engel, J.Stetefeld, S.Grzesiek.
 
  ABSTRACT  
 
Cellular adhesion by classical cadherins depends critically on the exact proteolytic removal of their N-terminal prosequences. In this combined solution NMR and X-ray crystallographic study, the consequences of propeptide cleavage of an epithelial cadherin construct (domains 1 and 2) were followed at atomic level. At low protein concentration, the N-terminal processing induces docking of the tryptophan-2 side-chain into a binding pocket on the same molecule. At high concentration, cleavage induces dimerization (KD=0.72 mM, k(off)=0.7 s(-1)) and concomitant intermolecular exchange of the betaA-strands and the tryptophan-2 side-chains. Thus, the cleavage represents the switch from a nonadhesive to the functional form of cadherin.
 
  Selected figure(s)  
 
Figure 1.
Figure 1 Schematic representation of prodomain -CAD1 domain boundaries of wild-type murine E-cadherin and E-cadherin constructs used in this study. The cleavage site of the prodomain in the wild-type protein is indicated by a black arrow. In HisXa-ECAD12, this cleavage site is mimicked by the factor Xa cleavage sequence IEGR (gray arrow). 		Figure 7.
Figure 7 Comparison of the ECAD12, M-ECAD12, and CCAD1 -5 crystal structures. The interacting monomers are shown in blue and yellow with their respective N-termini in red and green. The W2 residue is shown as space-fill. For better comparison, the blue CAD12 domains are shown in the same orientation for all three structures. Calcium atoms are indicated in magenta.
 
  The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2004, 23, 1699-1708) copyright 2004.  
  Figures were selected by the author.  

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
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.  
20190755 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, and L.Shapiro (2010).
T-cadherin structures reveal a novel adhesive binding mechanism.
  Nat Struct Mol Biol, 17, 339-347.
PDB codes: 3k5r 3k5s 3k6d 3k6f 3k6i
20679223 D.Schreiner, and J.A.Weiner (2010).
Combinatorial homophilic interaction between gamma-protocadherin multimers greatly expands the molecular diversity of cell adhesion.
  Proc Natl Acad Sci U S A, 107, 14893-14898.  
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
20190754 O.J.Harrison, F.Bahna, P.S.Katsamba, X.Jin, J.Brasch, J.Vendome, G.Ahlsen, K.J.Carroll, S.R.Price, B.Honig, and L.Shapiro (2010).
Two-step adhesive binding by classical cadherins.
  Nat Struct Mol Biol, 17, 348-357.
PDB codes: 3lnd 3lne 3lnf 3lng 3lnh 3lni
20457762 Y.Sugawara, T.Matsumura, Y.Takegahara, Y.Jin, Y.Tsukasaki, M.Takeichi, and Y.Fujinaga (2010).
Botulinum hemagglutinin disrupts the intercellular epithelial barrier by directly binding E-cadherin.
  J Cell Biol, 189, 691-700.  
20876147 Y.Wu, X.Jin, O.Harrison, L.Shapiro, B.H.Honig, and A.Ben-Shaul (2010).
Cooperativity between trans and cis interactions in cadherin-mediated junction formation.
  Proc Natl Acad Sci U S A, 107, 17592-17597.  
19846557 H.B.Guo, H.Johnson, M.Randolph, and M.Pierce (2009).
Regulation of homotypic cell-cell adhesion by branched N-glycosylation of N-cadherin extracellular EC2 and EC3 domains.
  J Biol Chem, 284, 34986-34997.  
19935869 L.Raptis, R.Arulanandam, A.Vultur, M.Geletu, S.Chevalier, and H.Feracci (2009).
Beyond structure, to survival: activation of Stat3 by cadherin engagement.
  Biochem Cell Biol, 87, 835-843.  
  20066110 L.Shapiro, and W.I.Weis (2009).
Structure and biochemistry of cadherins and catenins.
  Cold Spring Harbor Perspect Biol, 1, a003053.  
19553217 P.Katsamba, K.Carroll, G.Ahlsen, F.Bahna, J.Vendome, S.Posy, M.Rajebhosale, S.Price, T.M.Jessell, A.Ben-Shaul, L.Shapiro, and B.H.Honig (2009).
Linking molecular affinity and cellular specificity in cadherin-mediated adhesion.
  Proc Natl Acad Sci U S A, 106, 11594-11599.  
19604491 Y.Li, M.Hofmann, Q.Wang, L.Teng, L.K.Chlewicki, H.Pircher, and R.A.Mariuzza (2009).
Structure of natural killer cell receptor KLRG1 bound to E-cadherin reveals basis for MHC-independent missing self recognition.
  Immunity, 31, 35-46.
PDB codes: 3ff7 3ff8 3ff9
19114658 Y.Zhang, S.Sivasankar, W.J.Nelson, and S.Chu (2009).
Resolving cadherin interactions and binding cooperativity at the single-molecule level.
  Proc Natl Acad Sci U S A, 106, 109-114.  
18491227 F.Zhou, J.Su, L.Fu, Y.Yang, L.Zhang, L.Wang, H.Zhao, D.Zhang, Z.Li, and X.Zha (2008).
Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD.
  Glycoconj J, 25, 727-740.  
17945508 J.M.Benjamin, and W.J.Nelson (2008).
Bench to bedside and back again: molecular mechanisms of alpha-catenin function and roles in tumorigenesis.
  Semin Cancer Biol, 18, 53-64.  
18633485 M.P.Stemmler (2008).
Cadherins in development and cancer.
  Mol Biosyst, 4, 835-850.  
18326636 M.Sotomayor, and K.Schulten (2008).
The allosteric role of the Ca2+ switch in adhesion and elasticity of C-cadherin.
  Biophys J, 94, 4621-4633.  
18550521 S.A.Dames, E.Bang, D.Haüssinger, T.Ahrens, J.Engel, and S.Grzesiek (2008).
Insights into the Low Adhesive Capacity of Human T-cadherin from the NMR Structure of Its N-terminal Extracellular Domain.
  J Biol Chem, 283, 23485-23495.
PDB code: 2v37
18395225 S.Posy, L.Shapiro, and B.Honig (2008).
Sequence and structural determinants of strand swapping in cadherin domains: do all cadherins bind through the same adhesive interface?
  J Mol Biol, 378, 954-968.  
18682221 V.Z.Miloushev, F.Bahna, C.Ciatto, G.Ahlsen, B.Honig, L.Shapiro, and A.G.Palmer (2008).
Dynamic properties of a type II cadherin adhesive domain: implications for the mechanism of strand-swapping of classical cadherins.
  Structure, 16, 1195-1205.  
17850815 E.Parisini, J.M.Higgins, J.H.Liu, M.B.Brenner, and J.H.Wang (2007).
The crystal structure of human E-cadherin domains 1 and 2, and comparison with other cadherins in the context of adhesion mechanism.
  J Mol Biol, 373, 401-411.
PDB code: 2o72
17347145 H.Tsuiji, L.Xu, K.Schwartz, and B.M.Gumbiner (2007).
Cadherin conformations associated with dimerization and adhesion.
  J Biol Chem, 282, 12871-12882.  
17600523 L.Shapiro, J.Love, and D.R.Colman (2007).
Adhesion molecules in the nervous system: structural insights into function and diversity.
  Annu Rev Neurosci, 30, 451-474.  
17761538 R.B.Troyanovsky, O.Laur, and S.M.Troyanovsky (2007).
Stable and unstable cadherin dimers: mechanisms of formation and roles in cell adhesion.
  Mol Biol Cell, 18, 4343-4352.  
17539752 S.Pokutta, and W.I.Weis (2007).
Structure and mechanism of cadherins and catenins in cell-cell contacts.
  Annu Rev Cell Dev Biol, 23, 237-261.  
16834557 D.Leckband, and A.Prakasam (2006).
Mechanism and dynamics of cadherin adhesion.
  Annu Rev Biomed Eng, 8, 259-287.  
16980367 F.Cailliez, and R.Lavery (2006).
Dynamics and stability of E-cadherin dimers.
  Biophys J, 91, 3964-3971.  
16326909 M.V.Bayas, A.Leung, E.Evans, and D.Leckband (2006).
Lifetime measurements reveal kinetic differences between homophilic cadherin bonds.
  Biophys J, 90, 1385-1395.  
16564015 S.D.Patel, C.Ciatto, C.P.Chen, F.Bahna, M.Rajebhosale, N.Arkus, I.Schieren, T.M.Jessell, B.Honig, S.R.Price, and L.Shapiro (2006).
Type II cadherin ectodomain structures: implications for classical cadherin specificity.
  Cell, 124, 1255-1268.
PDB codes: 1zvn 1zxk 2a4c 2a4e 2a62
15937105 C.P.Chen, S.Posy, A.Ben-Shaul, L.Shapiro, and B.H.Honig (2005).
Specificity of cell-cell adhesion by classical cadherins: Critical role for low-affinity dimerization through beta-strand swapping.
  Proc Natl Acad Sci U S A, 102, 8531-8536.  
16183887 F.Cailliez, and R.Lavery (2005).
Cadherin mechanics and complexation: the importance of calcium binding.
  Biophys J, 89, 3895-3903.  
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.

 

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