› 5ms9

Solution NMR

Solution structure of Human Fibrillin-1 EGF2-EGF3-Hybrid1-cbEGF1 four domain fragment

Released:
DOI: 10.2210/pdb5ms9/pdb
PDB entry 5ms9 coloured by chain, ensemble of 20 models, front view.
PDB entry 5ms9 coloured by chain, ensemble of 20 models, side view.
PDB entry 5ms9 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
The N-Terminal Region of Fibrillin-1 Mediates a Bipartite Interaction with LTBP1.
Robertson IB, Dias HF, Osuch IH, Lowe ED, Jensen SA, Redfield C, Handford PA
Structure 25 1208-1221.e5 (2017)
PMID: 28669633

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152940 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fibrillin-1 Chain: A
Molecule details ›
Chain: A
Length: 177 amino acids
Theoretical weight: 18.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P35555 (Residues: 113-287; Coverage: 6%)
Gene names: FBN, FBN1
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 82%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Signaling Mechanisms of Myofibroblastic Activation: Outside-in and Inside-Out.
Zent et al. (2018)
2 more

3 mentions without citation

The N-Terminal Region of Fibrillin-1 Mediates a Bipartite Interaction with LTBP1.
Robertson et al. (2017)
2 more