› 1ale

Solution NMR

CONFORMATION OF TWO PEPTIDES CORRESPONDING TO HUMAN APOLIPOPROTEIN C-I RESIDUES 7-24 AND 35-53 IN THE PRESENCE OF SODIUM DODECYLSULFATE BY CD AND NMR SPECTROSCOPY

Released:
DOI: 10.2210/pdb1ale/pdb
PDB entry 1ale coloured by chain, ensemble of 5 models, front view.
PDB entry 1ale coloured by chain, ensemble of 5 models, side view.
PDB entry 1ale coloured by chain, ensemble of 5 models, top view.
Source organism: Homo sapiens
Primary publication:
Conformation of two peptides corresponding to human apolipoprotein C-I residues 7-24 and 35-53 in the presence of sodium dodecyl sulfate by CD and NMR spectroscopy.
Rozek A, Buchko GW, Cushley RJ
Biochemistry 34 7401-8 (1995)
PMID: 7779782

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-526752 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Truncated apolipoprotein C-I Chain: A
Molecule details ›
Chain: A
Length: 18 amino acids
Theoretical weight: 2.08 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P02654 (Residues: 33-50; Coverage: 32%)
Gene name: APOC1
Sequence domains: Apolipoprotein C-I (ApoC-1)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

9 review citations

Role of ApoCs in lipoprotein metabolism: functional differences between ApoC1, ApoC2, and ApoC3.
Jong et al. (1999)
8 more

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)