1TIT

TITIN, IG REPEAT 27, NMR, MINIMIZED AVERAGE STRUCTURE


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Submitted: 

wwPDB Validation   3D Report Full Report

Currently 1TIT does not have a validation slider image.


This is version 1.3 of the entry. See complete history


Literature

Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity.

Improta, S.Politou, A.S.Pastore, A.

(1996) Structure 4: 323-337

  • DOI: https://doi.org/10.1016/s0969-2126(96)00036-6
  • Primary Citation of Related Structures:  
    1TIT, 1TIU

  • PubMed Abstract: 

    The giant muscle protein titin forms a filament which spans half of the sarcomere and performs, along its length, quite diverse functions. The region of titin located in the sarcomere I-band is believed to play a major role in extensibility and passive elasticity of muscle. In the I-band, the titin sequence consists mostly of repetitive motifs of tandem immunoglobulin-like (Ig) modules intercalated by a potentially non-globular region. The highly repetitive titin architecture suggests that the molecular basis of its mechanical properties be approached through the characterization of the isolated components of the I-band and their interfaces. In the present paper, we report on the structure determination in solution of a representative Ig module from the I-band (I27) as solved by NMR techniques.


  • Organizational Affiliation

    EMBL, Meyerhofstrasse 1, D-69012 Heidelberg, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TITIN, I2798Homo sapiensMutation(s): 0 
Gene Names: TITIN GENE
UniProt & NIH Common Fund Data Resources
Find proteins for Q8WZ42 (Homo sapiens)
Explore Q8WZ42 
Go to UniProtKB:  Q8WZ42
PHAROS:  Q8WZ42
GTEx:  ENSG00000155657 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8WZ42
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Submitted: 

Structure Validation

View Full Validation Report

Currently 1TIT does not have a validation slider image.



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1996-07-11
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-03-02
    Changes: Database references, Derived calculations, Other