 |
PDBsum entry 3p5b
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Hydrolase/lipid binding protein
|
PDB id
|
|
|
|
3p5b
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
92 a.a.
|
|
|
|
|
|
|
|
|
|
|
493 a.a.
|
|
|
|
|
|
|
|
|
|
|
394 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Mechanistic implications for ldl receptor degradation from the pcsk9/ldlr structure at neutral ph.
|
|
|
Authors
|
|
P.Lo surdo,
M.J.Bottomley,
A.Calzetta,
E.C.Settembre,
A.Cirillo,
S.Pandit,
Y.G.Ni,
B.Hubbard,
A.Sitlani,
A.Carfí.
|
|
|
Ref.
|
|
Embo Rep, 2011,
12,
1300-1305.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Abstract
|
|
|
The protein PCSK9 (proprotein convertase subtilisin/kexin type 9) is a key
regulator of low-density lipoprotein receptor (LDLR) levels and cardiovascular
health. We have determined the crystal structure of LDLR bound to PCSK9 at
neutral pH. The structure shows LDLR in a new extended conformation. The PCSK9
C-terminal domain is solvent exposed, enabling cofactor binding, whereas the
catalytic domain and prodomain interact with LDLR epidermal growth factor(A) and
β-propeller domains, respectively. Thus, PCSK9 seems to hold LDLR in an
extended conformation and to interfere with conformational rearrangements
required for LDLR recycling.
|
|
|
|
|
|
|
