› 1bku

Solution NMR

EFFECTS OF GLYCOSYLATION ON THE STRUCTURE AND DYNAMICS OF EEL CALCITONIN, NMR, 10 STRUCTURES

Released:
DOI: 10.2210/pdb1bku/pdb
PDB entry 1bku coloured by chain, ensemble of 10 models, front view.
PDB entry 1bku coloured by chain, ensemble of 10 models, side view.
PDB entry 1bku coloured by chain, ensemble of 10 models, top view.
Source organism: Anguilla japonica
Primary publication:
Effects of glycosylation on the structure and dynamics of eel calcitonin in micelles and lipid bilayers determined by nuclear magnetic resonance spectroscopy.
Hashimoto Y, Toma K, Nishikido J, Yamamoto K, Haneda K, Inazu T, Valentine KG, Opella SJ
Biochemistry 38 8377-84 (1999)
PMID: 10387083

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134135 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calcitonin Chain: A
Molecule details ›
Chain: A
Length: 33 amino acids
Theoretical weight: 3.42 KDa
Source organism: Anguilla japonica
Expression system: Not provided
UniProt:
  • Canonical: P01262 (Residues: 1-32; Coverage: 100%)
Sequence domains: Calcitonin / CGRP / IAPP family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry
Expression system: Not provided

Quick links

Citations

5 review citations

Intermedin, a novel calcitonin family peptide that exists in teleosts as well as in mammals: a comparison with other calcitonin/intermedin family peptides in vertebrates.
Chang et al. (2004)
4 more

3 mentions without citation

A strategy for reducing gross errors in the generalized Born models of implicit solvation.
Onufriev et al. (2011)
2 more