 |
PDBsum entry 1dzi
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structural basis of collagen recognition by integrin alpha2beta1.
|
|
|
Authors
|
|
J.Emsley,
C.G.Knight,
R.W.Farndale,
M.J.Barnes,
R.C.Liddington.
|
|
|
Ref.
|
|
Cell, 2000,
101,
47-56.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
We have determined the crystal structure of a complex between the I domain of
integrin alpha2beta1 and a triple helical collagen peptide containing a critical
GFOGER motif. Three loops on the upper surface of the I domain that coordinate a
metal ion also engage the collagen, with a collagen glutamate completing the
coordination sphere of the metal. Comparison with the unliganded I domain
reveals a change in metal coordination linked to a reorganization of the upper
surface that together create a complementary surface for binding collagen.
Conformational changes propagate from the upper surface to the opposite pole of
the domain, suggesting both a basis for affinity regulation and a pathway for
signal transduction. The structural features observed here may represent a
general mechanism for integrin-ligand recognition.
|
|
|
|
|
|
|
|
Figure 3.
Figure 3. Two Conformations of the Integrin α2-I Domain
|
|
Figure 4.
Figure 4. Comparison of Conformational Changes in the α2-
and αM-I Domains
|
|
|
|
|
|
The above figures are
reprinted
by permission from Cell Press:
Cell
(2000,
101,
47-56)
copyright 2000.
|
|
|
|
|
|
|
