 |
PDBsum entry 1m3c
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Protein binding
|
PDB id
|
|
|
|
1m3c
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Changing protein backbone topology: structural and dynamic consequences of the backbone cyclization in sh3 domain
|
|
|
Authors
|
|
F.H.Schumann,
R.Varadan,
P.P.Tayakuniyil,
J.B.Hall,
J.A.Camarero,
D.Fushman.
|
|
|
Ref.
|
|
To be Published ...
|
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Rescuing a destabilized protein fold through backbone cyclization.
|
|
|
Authors
|
|
J.A.Camarero,
D.Fushman,
S.Sato,
I.Giriat,
D.Cowburn,
D.P.Raleigh,
T.W.Muir.
|
|
|
Ref.
|
|
J Mol Biol, 2001,
308,
1045-1062.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Figure 1.
Figure 1. Structure of the N-terminal SH3 domain of the
c-Crk protein adapter (white) in complex with its poly-Pro
ligand (red)[19] showing the SH3 secondary structure elements
(blue) as well as the residues Glu135, Lys164 and Trp170.
|
|
Figure 6.
Figure 6. Amide region of the 2D 1H{15N} HSQC spectra at
500 MHz for (a), Crk[lin-wt], (b) Crk[circ-D], (c) Crk[lin-D]
and (d) Crk[lin-D]+peptide ligand.
|
|
|
|
|
|
The above figures are
reproduced from the cited reference
with permission from Elsevier
|
|
|
|
|
|
|
