 |
PDBsum entry 2fcw
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Lipid transport/endocytosis/chaperone
|
PDB id
|
|
|
|
2fcw
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structure of an ldlr-Rap complex reveals a general mode for ligand recognition by lipoprotein receptors.
|
|
|
Authors
|
|
C.Fisher,
N.Beglova,
S.C.Blacklow.
|
|
|
Ref.
|
|
Mol Cell, 2006,
22,
277-283.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Proteins of the low-density lipoprotein receptor (LDLR) family are remarkable in
their ability to bind an extremely diverse range of protein and lipoprotein
ligands, yet the basis for ligand recognition is poorly understood. Here, we
report the 1.26 A X-ray structure of a complex between a two-module region of
the ligand binding domain of the LDLR and the third domain of RAP, an escort
protein for LDLR family members. The RAP domain forms a three-helix bundle with
two docking sites, one for each LDLR module. The mode of recognition at each
site is virtually identical: three conserved, calcium-coordinating acidic
residues from each LDLR module encircle a lysine side chain protruding from the
second helix of RAP. This metal-dependent mode of electrostatic recognition,
together with avidity effects resulting from the use of multiple sites,
represents a general binding strategy likely to apply in the binding of other
basic ligands to LDLR family proteins.
|
|
|
|
|
|
|
|
Figure 2.
Figure 2. Interface between LA3-4 and RAP-D3
|
|
Figure 4.
Figure 4. Docking Model for ApoE Binding
|
|
|
|
|
|
The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2006,
22,
277-283)
copyright 2006.
|
|
|
|
|
|
|
