 |
PDBsum entry 2i1p
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Ligand binding protein
|
PDB id
|
|
|
|
2i1p
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Solution structure of the twelfth cysteine-Rich ligand-Binding repeat in rat megalin.
|
 |
|
Authors
|
 |
C.A.Wolf,
F.Dancea,
M.Shi,
V.Bade-Noskova,
H.Rüterjans,
D.Kerjaschki,
C.Lücke.
|
 |
|
Ref.
|
 |
J Biomol Nmr, 2007,
37,
321-328.
|
 |
|
PubMed id
|
 |
|
 |
 |
|
Abstract
|
 |
|
Megalin, an approx. 600 kDa transmembrane glycoprotein that acts as multi-ligand
transporter, is a member of the low density lipoprotein receptor gene family.
Several cysteine-rich repeats, each consisting of about 40 residues, are
responsible for the multispecific binding of ligands. The solution structure of
the twelfth cysteine-rich ligand-binding repeat with class A motif found in
megalin features two short beta-strands and two helical turns, yielding the
typical fold with a I-III, II-V and IV-VI disulfide bridge connectivity pattern
and a calcium coordination site at the C-terminal end. The resulting differences
in electrostatic surface potential compared to other ligand-binding modules of
this gene family, however, may be responsible for the functional divergence.
|
 |
|
|
|
|
 |