 |
PDBsum entry 4ofi
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Cell adhesion
|
PDB id
|
|
|
|
4ofi
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Cell adhesion
|
|
|
Title:
|
|
Crystal structure of duf (kirre) d1
|
|
Structure:
|
|
Kin of irre, isoform a. Chain: a, b, c, d, e, f, g, h. Fragment: d1, unp residues 81-185. Synonym: kin of irre, isoform b, kin of irre, isoform c, kin of irre, isoform d, kin of irre, isoform e, kin of irre, isoform f, kin of irre, isoform g. Engineered: yes
|
|
Source:
|
|
Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: cg3653, dmel_cg3653, duf (kirre), kirre. Expressed in: trichoplusia ni. Expression_system_taxid: 7111.
|
|
Resolution:
|
|
|
2.30Å
|
R-factor:
|
0.194
|
R-free:
|
0.243
|
|
|
Authors:
|
|
E.Ozkan,K.C.Garcia
|
|
Key ref:
|
|
E.Özkan
et al.
(2014).
Extracellular architecture of the SYG-1/SYG-2 adhesion complex instructs synaptogenesis.
Cell,
156,
482-494.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
14-Jan-14
|
Release date:
|
19-Feb-14
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
Q9W4T9
(Q9W4T9_DROME) -
Kin of irre, isoform A from Drosophila melanogaster
|
|
|
|
Seq:
Struc:
|
|
|
|
956 a.a.
105 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
 |
CATH domain |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Cell
156:482-494
(2014)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Extracellular architecture of the SYG-1/SYG-2 adhesion complex instructs synaptogenesis.
|
|
E.Özkan,
P.H.Chia,
R.R.Wang,
N.Goriatcheva,
D.Borek,
Z.Otwinowski,
T.Walz,
K.Shen,
K.C.Garcia.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
SYG-1 and SYG-2 are multipurpose cell adhesion molecules (CAMs) that have
evolved across all major animal taxa to participate in diverse physiological
functions, ranging from synapse formation to formation of the kidney filtration
barrier. In the crystal structures of several SYG-1 and SYG-2 orthologs and
their complexes, we find that SYG-1 orthologs homodimerize through a common,
bispecific interface that similarly mediates an unusual orthogonal docking
geometry in the heterophilic SYG-1/SYG-2 complex. C. elegans SYG-1's
specification of proper synapse formation in vivo closely correlates with the
heterophilic complex affinity, which appears to be tuned for optimal function.
Furthermore, replacement of the interacting domains of SYG-1 and SYG-2 with
those from CAM complexes that assume alternative docking geometries or the
introduction of segmental flexibility compromised synaptic function. These
results suggest that SYG extracellular complexes do not simply act as
"molecular velcro" and that their distinct structural features are
important in instructing synaptogenesis. PAPERFLICK:
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
