 |
PDBsum entry 1waa
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Metal binding protein
|
PDB id
|
|
|
|
1waa
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Mechanical network in titin immunoglobulin from force distribution analysis.
|
|
|
Authors
|
|
W.Stacklies,
M.C.Vega,
M.Wilmanns,
F.Gräter.
|
|
|
Ref.
|
|
Plos Comput Biol, 2009,
5,
e1000306.
|
|
|
PubMed id
|
|
|
|
|
Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
|
|
|
|
Abstract
|
|
|
The role of mechanical force in cellular processes is increasingly revealed by
single molecule experiments and simulations of force-induced transitions in
proteins. How the applied force propagates within proteins determines their
mechanical behavior yet remains largely unknown. We present a new method based
on molecular dynamics simulations to disclose the distribution of strain in
protein structures, here for the newly determined high-resolution crystal
structure of I27, a titin immunoglobulin (IG) domain. We obtain a sparse,
spatially connected, and highly anisotropic mechanical network. This allows us
to detect load-bearing motifs composed of interstrand hydrogen bonds and
hydrophobic core interactions, including parts distal to the site to which force
was applied. The role of the force distribution pattern for mechanical stability
is tested by in silico unfolding of I27 mutants. We then compare the observed
force pattern to the sparse network of coevolved residues found in this family.
We find a remarkable overlap, suggesting the force distribution to reflect
constraints for the evolutionary design of mechanical resistance in the IG
family. The force distribution analysis provides a molecular interpretation of
coevolution and opens the road to the study of the mechanism of signal
propagation in proteins in general.
|
|
|
|
|
|
|
