Báo cáo khoa học: X-ray structure of glucose/galactose receptor from Salmonella typhimurium in complex with the physiological ligand, (2R)-glyceryl-b-D-galactopyranoside pdf
... protein. This kind of protein is exemplified by the
Thermus thermophilus protein, PDB entry 2B3B [28].
The mode of binding the monosaccharide is completely
different in terms of orientation of the ... calcium site of domain 2 was described
earlier, and tight binding of the ion was shown to con-
tribute to the integrity of the protein structure [17,22].
The sod...
... conformation. At the N-terminus of the
peptide, the alignment diverges more, with the major
difference being that the N-terminal Met is signifi-
cantly further away from the binding cleft in the
CTPR390–MEEVD ... complexes are in
the location of the peptide chains relative to the pro-
tein (Fig. 5A). The Hsp90 peptide is located in the
CTPR390 concave clef...
... calculations
for the two interacting molecular surfaces, performed
with the program sc from the ccp4 suite [27]. The
obtained sc value of 0.400 indicates weak binding of
the two entities of the RATE. Therefore, ... of RNase molecules
on the cell surface), thereby favoring their endocytosis
[19]. The stoichiometry of RI binding to RATEs and
the role of the R...
... elsewhere on the
pathway of the multistep catalysis, where the OH inter-
actions with residues of the active site are not required.
Using information on the 3D structure of the enzyme–
inhibitor complex, ... structures [24]. Parallel studies of these effects
allowed identification of the specific interactions between
the inhibitors and the proteins. In the a...
... data. The accu-
racy of the structure calculated without these constraints is,
however, supported by the similarities of the 800 MHz
structures of the a-domain of mouse MT1 compared to the
one ... to the average minimized structure,
for each set of reintroduced long-range NOEs. Determining
the deviation of the generated structure with a reduced
number of...
... The bind-
ing of the ®rst CN
±
ligand to the iron was thus more easy in
the hydrophobic binding pocket of the antibody than the
binding of the second one, most probably because of the
steric hindrance ... substituents
of the meso-phenyl rings being recognized by th e side chains
of amino acids of the antibody [36]; (b) in the case of 13G10,
one carbox...
... those in the “input queue,” and
if not, shifting a word from the input queue onto the
processing buffer. The distinction is marked, in our
notation, by a |: the words and trees before | are in
the ... if
there is another displaced item in the tree containing
the original CH that is compatible with the UNCH
feature but displaced from some other phrase. This
requ...
... gives the solvent
access to the trinuclear centre. However, the channel is
blocked by the C-terminal end of the amino acid chain
in MaL ⁄rMaL [25,33]. Similarly, in the structure of
TaLcc1, the ... DSGL as the last four amino acids
penetrating into the channel.
The C-terminal processing has been reported for
asco-laccases of different origins [37–39]; furthermo...
... determined the X-ray crystal structure of a truncated form
of importin-a lacking the importin-b binding domain, bound to a CLIC4
NLS peptide. The NLS peptide binds to the major binding site in an
extended ... cargo binding sites, referred to as
the major and minor binding sites [1]. These sites are
located in the concave face of the protein near regions
of invari...
... metal-binding site
at the interface of the two domains, which consists
of four side chains: two (His31 and His79) from the
N-terminal domain and two (Asp165 and His169) from
the C-terminal domain ... focus
on the coordination of the metal cofactor in the active
site as well as the changes it experiences in response to
different metal cofactors. Finally, by compar...