Javascript verkar inte påslaget? - Vissa delar av Lunds universitets webbplats fungerar inte optimalt utan javascript, kontrollera din webbläsares inställningar.
Du är här

Structural studies of metal-binding proteins revealing dynamic behaviour

Publiceringsår: 2001
Språk: Engelska
Sidor: 100
Dokumenttyp: Doktorsavhandling
Förlag: Molecular biophysics (S)


The Mg2+ and Mn2+ structures of calbindin D9k have been determined and they reveal a conformational change compared to the structures of apo and (Ca2+)2-calbindin D9k. These findings are unique, since normally calcium and not magnesium is known to induce conformational changes of EF-hand proteins. It has also been shown that calbindin D9k binds one Mg2+ (Kd=1mM) in the regular C-terminal EF-hand close to physiological conditions. The binding of Mg2+ decreases the affinity for Ca2+, 5-fold and vice versa.

Two apo staphylococcal enterotoxin H (SEH) structures and one ZnSEH structure have been determined. The structures reveal that SEH lacks the SEB-like binding to MHC class II. Based upon structural differences for the same protein a novel mechanism for SEH recognition of different TcR Vbeta is suggested. The ZnSEH structure together with the homodimers of SEH formed by the crystal packing in two crystal forms imply the approximate area used for Zn2+-dependent binding to MHC class II.

A dimeric form of calbindin D9k has been found. The C-terminal EF-hand of one monomer packs towards the N-terminal EF-hand of the other monomer and vice versa. The dimerisation is primarily caused by the P43M substitution in the linker region between the EF-hands and low pH (= 5.0). The P43M substitution may facilitate 3D domain swapping in two ways; by inducing an extended hydrophobic core in the dimeric form of calbindin D9k and by stabilizing a partially unfolded form of calbindin D9k .

The structure of staphylococcal enterotoxin A (SEA) with the substitution H187A (SEAH187A) has been determined. SEAH187A has previously been shown to give rise to reduced affinity for Zn2+ and a 10-fold decrease in Zn2+-dependent binding to MHC class II. The structure and aggregation analyses reveal the importance of additional ligands for SEAH187A to bind Zn2+ at low physiological Zn2+ concentrations.


K:A at the Center of Chemistry and Chemical Engineering
  • E Yvonne Jones


  • Biological Sciences
  • Kemi
  • Chemistry
  • Molekylär biofysik
  • Molecular biophysics
  • zinc
  • magnesium
  • superantigen
  • calbindin D9k
  • X-ray crystallography
  • staphylococcal enterotoxin
  • structure
  • Chemical technology and engineering
  • Kemiteknik och kemisk teknologi


Box 117, 221 00 LUND
Telefon 046-222 00 00 (växel)
Telefax 046-222 47 20
lu [at] lu [dot] se

Fakturaadress: Box 188, 221 00 LUND
Organisationsnummer: 202100-3211
Om webbplatsen