 |
PDBsum entry 2kax
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Metal binding protein
|
PDB id
|
|
|
|
2kax
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Solution structure and dynamics of s100a5 in the apo and ca2+-Bound states.
|
|
|
Authors
|
|
I.Bertini,
S.Das gupta,
X.Hu,
T.Karavelas,
C.Luchinat,
G.Parigi,
J.Yuan.
|
|
|
Ref.
|
|
J Biol Inorg Chem, 2009,
14,
1097-1107.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
S100A5 is a calcium binding protein of the S100 family, with one canonical and
one S100-specific EF-hand motif per subunit. Although its function is still
unknown, it has recently been reported to be one of the S100 proteins able to
interact with the receptor for advanced glycation end products. The homodimeric
solution structures of S100A5 in both the apo and the calcium(II)-loaded forms
have been obtained, and show a conformational rearrangement upon calcium
binding. This rearrangement involves, in particular, the hinge loop connecting
the N-terminal and the C-terminal EF-hand domains, the reorientation of helix
III with respect to helix IV, as common to several S100 proteins, and the
elongation of helix IV. The details of the structural changes are important
because they must be related to the different functions, still largely unknown,
of the different members of the S100 family. For the first time for a
full-length S100 protein, relaxation measurements were performed on both the apo
and the calcium-bound forms. A quite large mobility was observed in the hinge
loop, which is not quenched in the calcium form. The structural differences
resulting upon calcium binding change the global shape and the distribution of
hydrophobic and charged residues of the S100A5 homodimer in a modest but
significantly different manner with respect to the closest homologues S100A4 and
S100A6.
|
|
|
|
|
|
|
