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PDBsum entry 2iak

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protein ligands links
Cell adhesion PDB id
2iak
Jmol
Contents
Protein chain
198 a.a. *
Ligands
SO4 ×2
Waters ×11
* Residue conservation analysis
PDB id:
2iak
Name: Cell adhesion
Title: Crystal structure of a protease resistant fragment of the pl domain of bullous pemphigoid antigen1 (bpag1)
Structure: Bullous pemphigoid antigen 1, isoform 5. Chain: a. Fragment: plakin domain, residues 226-449. Synonym: bpa, hemidesmosomal plaque protein, dystonia muscu protein, dystonin. Engineered: yes. Mutation: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: dst, bpag1. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Resolution:
3.00Å     R-factor:   0.228     R-free:   0.267
Authors: J.J.Jefferson
Key ref:
J.J.Jefferson et al. (2007). Structural analysis of the plakin domain of bullous pemphigoid antigen1 (BPAG1) suggests that plakins are members of the spectrin superfamily. J Mol Biol, 366, 244-257. PubMed id: 17161423 DOI: 10.1016/j.jmb.2006.11.036
Date:
08-Sep-06     Release date:   28-Nov-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q91ZU6  (DYST_MOUSE) -  Dystonin
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7393 a.a.
198 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 

 
DOI no: 10.1016/j.jmb.2006.11.036 J Mol Biol 366:244-257 (2007)
PubMed id: 17161423  
 
 
Structural analysis of the plakin domain of bullous pemphigoid antigen1 (BPAG1) suggests that plakins are members of the spectrin superfamily.
J.J.Jefferson, C.Ciatto, L.Shapiro, R.K.Liem.
 
  ABSTRACT  
 
Bullous pemphigoid antigen 1 (BPAG1) is a member of the plakin family of proteins. The plakins are multi-domain proteins that have been shown to interact with microtubules, actin filaments and intermediate filaments, as well as proteins found in cellular junctions. These interactions are mediated through different domains on the plakins. The interactions between plakins and components of specialized cell junctions such as desmosomes and hemidesmosomes are mediated through the so-called plakin domain, which is a common feature of the plakins. We report the crystal structure of a stable fragment from BPAG1, residues 226-448, defined by limited proteolysis of the whole plakin domain. The structure, determined by single-wavelength anomalous diffraction phasing from a selenomethionine-substituted crystal at 3.0 A resolution, reveals a tandem pair of triple helical bundles closely related to spectrin repeats. Based on this structure and analysis of sequence conservation, we propose that the architecture of plakin domains is defined by two pairs of spectrin repeats interrupted by a putative Src-Homology 3 (SH3) domain.
 
  Selected figure(s)  
 
Figure 2.
Figure 2. Structure of the spectrin repeats identified within the plakin domain of BPAG1. (a) A cartoon representation of the structure showing a loop-like region (in green) at the extreme N terminus followed by a pair of spectrin repeats (repeat 1 in red and repeat 2 in blue) in tandem connected by a linker region (L in magenta) that is also helical in nature. The structure consists of helices A, B and C (repeat 1) and helices D, E and F (repeat 2). (b) A stereo diagram showing all atoms of the structure shown in (a).
Figure 3.
 
  The above figures are reprinted from an Open Access publication published by Elsevier: J Mol Biol (2007, 366, 244-257) copyright 2007.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21464301 A.Al-Amoudi, D.Castaño-Diez, D.P.Devos, R.B.Russell, G.T.Johnson, and A.S.Frangakis (2011).
The three-dimensional molecular structure of the desmosomal plaque.
  Proc Natl Acad Sci U S A, 108, 6480-6485.  
20101027 J.J.Ipsaro, and A.Mondragón (2010).
Structural basis for spectrin recognition by ankyrin.
  Blood, 115, 4093-4101.
PDB codes: 3kbt 3kbu
19141864 J.J.Ipsaro, L.Huang, and A.Mondragón (2009).
Structures of the spectrin-ankyrin interaction binding domains.
  Blood, 113, 5385-5393.
PDB codes: 3f57 3f59
  19736524 J.M.de Pereda, E.Ortega, N.Alonso-García, M.Gómez-Hernández, and A.Sonnenberg (2009).
Advances and perspectives of the architecture of hemidesmosomes: lessons from structural biology.
  Cell Adh Migr, 3, 361-364.  
19168783 P.R.Stabach, I.Simonović, M.A.Ranieri, M.S.Aboodi, T.A.Steitz, M.Simonovi, and J.S.Morrow (2009).
The structure of the ankyrin-binding site of beta-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties.
  Blood, 113, 5377-5384.
PDB code: 3edu
19366731 R.Bhattacharya, A.M.Gonzalez, P.J.Debiase, H.E.Trejo, R.D.Goldman, F.W.Flitney, and J.C.Jones (2009).
Recruitment of vimentin to the cell surface by beta3 integrin and plectin mediates adhesion strength.
  J Cell Sci, 122, 1390-1400.  
18386043 J.Waschke (2008).
The desmosome and pemphigus.
  Histochem Cell Biol, 130, 21-54.  
18682224 T.Pavkov, E.M.Egelseer, M.Tesarz, D.I.Svergun, U.B.Sleytr, and W.Keller (2008).
The structure and binding behavior of the bacterial cell surface layer protein SbsC.
  Structure, 16, 1226-1237.
PDB code: 2ra1
17849487 K.G.Young, and R.Kothary (2007).
Dystonin/Bpag1--a link to what?
  Cell Motil Cytoskeleton, 64, 897-905.  
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 codes are shown on the right.