› 2mom

Solution NMR

Structural insights of TM domain of LAMP-2A in DPC micelles

Released:
DOI: 10.2210/pdb2mom/pdb
PDB entry 2mom coloured by chain, ensemble of 20 models, front view.
PDB entry 2mom coloured by chain, ensemble of 20 models, side view.
PDB entry 2mom coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structure of transmembrane domain of lysosome-associated membrane protein type 2a (LAMP-2A) reveals key features for substrate specificity in chaperone-mediated autophagy.
Rout AK, Strub MP, Piszczek G, Tjandra N
J Biol Chem 289 35111-23 (2014)
PMID: 25342746

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146599 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysosome-associated membrane glycoprotein 2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 42 amino acids
Theoretical weight: 4.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P13473 (Residues: 369-410; Coverage: 11%)
Gene name: LAMP2
Sequence domains: Lysosome-associated membrane glycoprotein 2, transmembrane segment

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 32%
Refinement method: distance geometry, simulated annealing, torsion angle dynamics
Expression system: Escherichia coli

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Citations

24 review citations

The coming of age of chaperone-mediated autophagy.
Kaushik et al. (2018)
23 more

7 mentions without citation

Bcl-2 enhances Ca(2+) signaling to support the intrinsic regenerative capacity of CNS axons.
Jiao et al. (2005)
6 more