6FWX

Chimeric titin Z1Z2-Z1Z2 tandem (Z1212) functionalized with a GRGDS exogenous peptide from fibronectin


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.226 
  • R-Value Work: 0.200 
  • R-Value Observed: 0.201 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Self-Assembling Proteins as High-Performance Substrates for Embryonic Stem Cell Self-Renewal.

Hill, C.J.Fleming, J.R.Mousavinejad, M.Nicholson, R.Tzokov, S.B.Bullough, P.A.Bogomolovas, J.Morgan, M.R.Mayans, O.Murray, P.

(2019) Adv Mater 31: e1807521-e1807521

  • DOI: https://doi.org/10.1002/adma.201807521
  • Primary Citation of Related Structures:  
    6FWX

  • PubMed Abstract: 

    The development of extracellular matrix mimetics that imitate niche stem cell microenvironments and support cell growth for technological applications is intensely pursued. Specifically, mimetics are sought that can enact control over the self-renewal and directed differentiation of human pluripotent stem cells (hPSCs) for clinical use. Despite considerable progress in the field, a major impediment to the clinical translation of hPSCs is the difficulty and high cost of large-scale cell production under xeno-free culture conditions using current matrices. Here, a bioactive, recombinant, protein-based polymer, termed ZT Fn , is presented that closely mimics human plasma fibronectin and serves as an economical, xeno-free, biodegradable, and functionally adaptable cell substrate. The ZT Fn substrate supports with high performance the propagation and long-term self-renewal of human embryonic stem cells while preserving their pluripotency. The ZT Fn polymer can, therefore, be proposed as an efficient and affordable replacement for fibronectin in clinical grade cell culturing. Further, it can be postulated that the ZT polymer has significant engineering potential for further orthogonal functionalization in complex cell applications.


  • Organizational Affiliation

    Department of Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, Nuffield Building, Crown Street, Liverpool, L69 3BX, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Titin,Titin,Titin
A, B
394Homo sapiensMutation(s): 0 
Gene Names: TTN
EC: 2.7.11.1
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
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.226 
  • R-Value Work: 0.200 
  • R-Value Observed: 0.201 
  • Space Group: H 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 134.4α = 90
b = 134.4β = 90
c = 134γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XDSdata scaling
PHENIXphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
BBRSC and JRI OrthopaedicsUnited KingdomBB/I01666X/1

Revision History  (Full details and data files)

  • Version 1.0: 2019-03-27
    Type: Initial release
  • Version 1.1: 2019-10-09
    Changes: Data collection, Database references
  • Version 1.2: 2020-04-08
    Changes: Database references
  • Version 1.3: 2024-01-17
    Changes: Data collection, Database references, Refinement description