PDBsum entry 1orq

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protein metals Protein-protein interface(s) links
Membrane protein PDB id
Jmol PyMol
Protein chains
215 a.a. *
219 a.a. *
223 a.a. *
_CD ×7
__K ×6
Waters ×6
* Residue conservation analysis
PDB id:
Name: Membrane protein
Title: X-ray structure of a voltage-dependent potassium channel in with an fab
Structure: 6e1 fab light chain. Chain: a. 6e1 fab heavy chain. Chain: b. Potassium channel. Chain: c. Fragment: kvap. Engineered: yes. Mutation: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Other_details: mouse hybridoma. Aeropyrum pernix. Organism_taxid: 56636. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dodecamer (from PDB file)
3.20Å     R-factor:   0.253     R-free:   0.298
Authors: Y.Jiang,A.Lee,J.Chen,V.Ruta,M.Cadene,B.T.Chait,R.Mackinnon
Key ref:
Y.Jiang et al. (2003). X-ray structure of a voltage-dependent K+ channel. Nature, 423, 33-41. PubMed id: 12721618 DOI: 10.1038/nature01580
14-Mar-03     Release date:   06-May-03    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P01837  (IGKC_MOUSE) -  Ig kappa chain C region
106 a.a.
215 a.a.
Protein chain
Pfam   ArchSchema ?
P01865  (GCAM_MOUSE) -  Ig gamma-2A chain C region, membrane-bound form
398 a.a.
219 a.a.*
Protein chain
Pfam   ArchSchema ?
Q9YDF8  (KVAP_AERPE) -  Voltage-gated potassium channel
295 a.a.
223 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     blood microparticle   6 terms 
  Biological process     transmembrane transport   11 terms 
  Biochemical function     antigen binding     4 terms  


DOI no: 10.1038/nature01580 Nature 423:33-41 (2003)
PubMed id: 12721618  
X-ray structure of a voltage-dependent K+ channel.
Y.Jiang, A.Lee, J.Chen, V.Ruta, M.Cadene, B.T.Chait, R.MacKinnon.
Voltage-dependent K+ channels are members of the family of voltage-dependent cation (K+, Na+ and Ca2+) channels that open and allow ion conduction in response to changes in cell membrane voltage. This form of gating underlies the generation of nerve and muscle action potentials, among other processes. Here we present the structure of KvAP, a voltage-dependent K+ channel from Aeropyrum pernix. We have determined a crystal structure of the full-length channel at a resolution of 3.2 A, and of the isolated voltage-sensor domain at 1.9 A, both in complex with monoclonal Fab fragments. The channel contains a central ion-conduction pore surrounded by voltage sensors, which form what we call 'voltage-sensor paddles'-hydrophobic, cationic, helix-turn-helix structures on the channel's outer perimeter. Flexible hinges suggest that the voltage-sensor paddles move in response to membrane voltage changes, carrying their positive charge across the membrane.
  Selected figure(s)  
Figure 3.
Figure 3: Architecture of the KvAP channel. a, Stereo image of the KvAP channel tetramer viewed from the intracellular side of the membrane. Each subunit is a different colour; helical elements of the blue subunit are labelled numerically for S1 -S6 and with P for the pore helix. N and C mark the termini. b, Stereo image of the KvAP channel tetramer viewed from the side with the intracellular solution below. Views in a and b are related by a 90 rotation about a horizontal axis. Side chains of selected residues known to be involved in voltage-dependent gating are shown on the blue and red subunits. Selected helical elements are labelled on the red and blue subunits. c, A single KvAP subunit viewed from the same perspective as in b. Conserved arginine residues on the voltage-sensor paddle are shown. d, A schematic diagram of the KvAP subunit topology is shown with an orange selectivity filter and an arrow to indicate the ion pathway. The demarcation between the S4 -S5 linker and S5 is indicated by a black line.
Figure 7.
Figure 7: Effect of Fabs on voltage-sensor conformation. a, Stereo view of two subunits (blue and red) from the full-length channel viewed from the side with the intracellular solution below. b, Identical view of the pore (S5 -S6) with the isolated voltage sensor docked according to the position of S2 in the full-length channel. The Asp 62 -Arg 133 salt bridge is shown.
  The above figures are reprinted by permission from Macmillan Publishers Ltd: Nature (2003, 423, 33-41) copyright 2003.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
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PDB code: 4dxw
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PDB code: 2kyh
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PDB code: 3org
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PDB code: 3inu
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