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PDBsum entry 1bpv

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protein links
Connectin PDB id
1bpv
Jmol
Contents
Protein chain
104 a.a. *
* Residue conservation analysis
PDB id:
1bpv
Name: Connectin
Title: Titin module a71 from human cardiac muscle, nmr, 50 structures
Structure: Titin. Chain: a. Fragment: 71 th domain from the a-band. Synonym: a71, connectin. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: heart. Tissue: muscle. Organelle: sarcomere. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 50 models
Authors: C.Muhle-Goll,A.Pastore,M.Nilges
Key ref:
C.M.Goll et al. (1998). The three-dimensional structure of a type I module from titin: a prototype of intracellular fibronectin type III domains. Structure, 6, 1291-1302. PubMed id: 9782056 DOI: 10.1016/S0969-2126(98)00129-4
Date:
11-Aug-98     Release date:   12-Aug-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q8WZ42  (TITIN_HUMAN) -  Titin
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34350 a.a.
104 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.7.11.1  - Non-specific serine/threonine protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein = ADP + a phosphoprotein
ATP
+ protein
= ADP
+ phosphoprotein
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1016/S0969-2126(98)00129-4 Structure 6:1291-1302 (1998)
PubMed id: 9782056  
 
 
The three-dimensional structure of a type I module from titin: a prototype of intracellular fibronectin type III domains.
C.M.Goll, A.Pastore, M.Nilges.
 
  ABSTRACT  
 
BACKGROUND: Titin is a huge protein ( approximately 3 MDa) that is present in the contractile unit (sarcomere) of striated muscle and has a key role in muscle assembly and elasticity. Titin is mainly composed of two types of module (type I and II). Type I modules are found exclusively in the region of titin localised in the A band, where they are arranged in a super-repeat pattern that correlates with the ultrastructure of the thick filament. No structure of a titin type I module has been reported so far. RESULTS: We have determined the structure of a representative type I module, A71, using nuclear magnetic resonance (NMR) spectroscopy. The structure has the predicted fibronectin type III fold. Titin-specific conserved residues are either located at the putative module-module interfaces or along one side of the protein surface. Several proline residues that contribute to two stretches in a polyproline II helix conformation are solvent-exposed and line up as a continuous ribbon extending over more than two-thirds of the module surface. Homology models of the type I module N-terminal to A71 (A70) and the double module A70-A71 were used to discuss possible intermodule interactions and their role in module-module orientation. CONCLUSIONS: As residues at the module-module interfaces are highly conserved, we speculate that similar interactions govern all of the interfaces between type I modules in titin. This conservation would lead to a regular multiple array of similar surface structures. Such an arrangement would allow arrays of contiguous type I modules to expose multiple proline stretches in a highly regular way and these may act as binding sites for other thick filament proteins.
 
  Selected figure(s)  
 
Figure 6.
Figure 6. The solvent-exposed surface of A71. The surface is displayed as white dots surrounding the CPK structure of A71. Exposed proline sidechains (coloured in yellow) and the adjacent hydrophobic patch of isoleucine residues (coloured in light green) are shown in solid surface representation.
 
  The above figure is reprinted by permission from Cell Press: Structure (1998, 6, 1291-1302) copyright 1998.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21050039 A.V.Mikelsaar, A.Sünter, P.Toomik, R.Mikelsaar, I.Kalev, A.Kõiveer, A.Piirsoo, K.Karpson, and E.Juronen (2010).
Titin A-band-specific monoclonal antibody Tit1 5H1.1. Cellular Titin as a centriolar protein in non-muscle cells.
  Hybridoma (Larchmt), 29, 391-401.  
20625501 L.Tskhovrebova, and J.Trinick (2010).
Roles of titin in the structure and elasticity of the sarcomere.
  J Biomed Biotechnol, 2010, 612482.  
  19789381 A.Kontrogianni-Konstantopoulos, M.A.Ackermann, A.L.Bowman, S.V.Yap, and R.J.Bloch (2009).
Muscle giants: molecular scaffolds in sarcomerogenesis.
  Physiol Rev, 89, 1217-1267.  
18022190 I.Lappalainen, M.G.Hurley, and J.Clarke (2008).
Plasticity within the obligatory folding nucleus of an immunoglobulin-like domain.
  J Mol Biol, 375, 547-559.  
16341830 M.Marino, D.I.Svergun, L.Kreplak, P.V.Konarev, B.Maco, D.Labeit, and O.Mayans (2005).
Poly-Ig tandems from I-band titin share extended domain arrangements irrespective of the distinct features of their modular constituents.
  J Muscle Res Cell Motil, 26, 355-365.  
15322090 L.Tskhovrebova, and J.Trinick (2004).
Properties of titin immunoglobulin and fibronectin-3 domains.
  J Biol Chem, 279, 46351-46354.  
15298915 M.C.Leake, D.Wilson, M.Gautel, and R.M.Simmons (2004).
The elasticity of single titin molecules using a two-bead optical tweezers assay.
  Biophys J, 87, 1112-1135.  
15211512 M.Cieplak, T.X.Hoang, and M.O.Robbins (2004).
Thermal effects in stretching of Go-like models of titin and secondary structures.
  Proteins, 56, 285-297.  
12444090 A.Kontrogianni-Konstantopoulos, and R.J.Bloch (2003).
The hydrophilic domain of small ankyrin-1 interacts with the two N-terminal immunoglobulin domains of titin.
  J Biol Chem, 278, 3985-3991.  
14506471 L.Tskhovrebova, and J.Trinick (2003).
Titin: properties and family relationships.
  Nat Rev Mol Cell Biol, 4, 679-689.  
12190614 T.Shen, L.S.Canino, and J.A.McCammon (2002).
Unfolding proteins under external forces: a solvable model under the self-consistent pair contact probability approximation.
  Phys Rev Lett, 89, 068103.  
11509370 J.G.Head, A.Houmeida, P.J.Knight, A.R.Clarke, J.Trinick, and R.L.Brady (2001).
Stability and folding rates of domains spanning the large A-band super-repeat of titin.
  Biophys J, 81, 1570-1579.  
10819994 R.A.Atkinson, C.Joseph, F.Dal Piaz, L.Birolo, G.Stier, P.Pucci, and A.Pastore (2000).
Binding of alpha-actinin to titin: implications for Z-disk assembly.
  Biochemistry, 39, 5255-5264.  
10047523 C.C.Gregorio, H.Granzier, H.Sorimachi, and S.Labeit (1999).
Muscle assembly: a titanic achievement?
  Curr Opin Cell Biol, 11, 18-25.  
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.