Polcalcins such as Bet v 4 and Phl p 7 are pollen allergens that are con-structed from EF-hand motifs, which are very common and well character-ized helix–loop–helix motifs with calcium-binding functions, as elementary
building blocks. Being members of an exceptionally well-characterized
protein superfamily, these allergens highlight the fundamental challenge in
explaining what features distinguish allergens from nonallergenic proteins.
It has been previously reported that the structure of a human pancreatic
ribonuclease variant, namely PM8, constitutes a dimer by the exchange of
an N-terminal domain, although in an aqueous solution it is found mainly
as a monomer. First, we investigated the solution conditions that favour
the dimerization of this variant.
Conformational diseases constitute a group of heterologous disorders in
which a constituent host protein undergoes changes in conformation, lead-ing to aggregation and deposition. To understand the molecular mecha-nisms of the process of amyloid fibril formation, numerousin vitro and
in vivo studies, including model and pathologically relevant proteins, have
The bacterial twin-arginine translocation (Tat) system is a protein targeting
pathway dedicated to the transport of folded proteins across the cytoplas-mic membrane. Proteins transported on the Tat pathway are synthesised as
precursors with N-terminal signal peptides containing a conserved amino
Bacterial cold shock proteins (CSPs) regulate cellular adaptation to cold
stress. Functions ascribed to CSP include roles as RNA chaperones and in
transcription antitermination. We present the crystal structure of the Bacil-lus caldolyticus CSP (Bc-Csp) in complex with hexathymidine (dT6)ata
resolution of 1.29 A
Although structurally similar, classic pancreatic lipase (PL) and pancreatic
lipase-related protein (PLRP)2, expressed in the pancreas of several species,
differ in substrate specificity, sensitivity to bile salts and colipase depen-dence. In order to investigate the role of the two domains of PLRP2 in the
function of the protein, two chimeric proteins were designed by swapping
the N and C structural domains between the horse PL (Nc and Cc
domains) and the horse PLRP2 (N2 and C2 domains).
As an effort to elucidate the quaternary structure of cyclomaltodextrinase
I-5 (CDase I-5) as a function of pH and salt concentration, the dissoci-ation/association processes of the enzyme were investigated under various
pH and salt conditions. Previous crystallographic analysis of CDase I-5
indicated that it existed exclusively as a dodecamer at pH 7.0, forming an
assembly of six 3D domain-swapped dimeric subunits.