 |
PDBsum entry 4ckh
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Signaling protein
|
PDB id
|
|
|
|
4ckh
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Signaling protein
|
|
|
Title:
|
|
Helical reconstruction of acap1(bar-ph domain) decorated membrane tubules by cryo-electron microscopy
|
|
Structure:
|
|
Arf-gap with coiled-coil, ank repeat and ph domain- containing protein 1. Chain: a, b, c, d. Fragment: bar-ph domain, residues 1-377. Synonym: centaurin-beta-1, cnt-b1, bar-ph domain of acap1. Engineered: yes
|
|
Source:
|
|
Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
|
|
Authors:
|
|
X.Y.Pang,J.Fan,Y.Zhang,K.Zhang,B.Q.Gao,J.Ma,J.Li,Y.C.Deng,Q.J.Zhou, V.Hsu,F.Sun
|
|
Key ref:
|
|
X.Pang
et al.
(2014).
A PH domain in ACAP1 possesses key features of the BAR domain in promoting membrane curvature.
Dev Cell,
31,
73-86.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
06-Jan-14
|
Release date:
|
15-Oct-14
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
Q15027
(ACAP1_HUMAN) -
Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 from Homo sapiens
|
|
|
|
Seq:
Struc:
|
|
|
|
740 a.a.
369 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Dev Cell
31:73-86
(2014)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
A PH domain in ACAP1 possesses key features of the BAR domain in promoting membrane curvature.
|
|
X.Pang,
J.Fan,
Y.Zhang,
K.Zhang,
B.Gao,
J.Ma,
J.Li,
Y.Deng,
Q.Zhou,
E.H.Egelman,
V.W.Hsu,
F.Sun.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
The BAR (Bin-Amphiphysin-Rvs) domain undergoes dimerization to produce a curved
protein structure, which superimposes onto membrane through electrostatic
interactions to sense and impart membrane curvature. In some cases, a BAR domain
also possesses an amphipathic helix that inserts into the membrane to induce
curvature. ACAP1 (Arfgap with Coil coil, Ankyrin repeat, and PH domain protein
1) contains a BAR domain. Here, we show that this BAR domain can neither bind
membrane nor impart curvature, but instead requires a neighboring PH (Pleckstrin
Homology) domain to achieve these functions. Specific residues within the PH
domain are responsible for both membrane binding and curvature generation. The
BAR domain adjacent to the PH domain instead interacts with the BAR domains of
neighboring ACAP1 proteins to enable clustering at the membrane. Thus, we have
uncovered the molecular basis for an unexpected and unconventional collaboration
between PH and BAR domains in membrane bending.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
