 |
PDBsum entry 4q3g
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
Structure of the osserk2 leucine-Rich repeat extracellular domain.
|
|
|
Authors
|
|
R.Mcandrew,
R.N.Pruitt,
S.G.Kamita,
J.H.Pereira,
D.Majumdar,
B.D.Hammock,
P.D.Adams,
P.C.Ronald.
|
|
|
Ref.
|
|
Acta Crystallogr D Biol Crystallogr, 2014,
70,
3080-3086.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Somatic embryogenesis receptor kinases (SERKs) are leucine-rich repeat
(LRR)-containing integral membrane receptors that are involved in the regulation
of development and immune responses in plants. It has recently been shown that
rice SERK2 (OsSERK2) is essential for XA21-mediated resistance to the pathogen
Xanthomonas oryzae pv. oryzae. OsSERK2 is also required for the BRI1-mediated,
FLS2-mediated and EFR-mediated responses to brassinosteroids, flagellin and
elongation factor Tu (EF-Tu), respectively. Here, crystal structures of the LRR
domains of OsSERK2 and a D128N OsSERK2 mutant, expressed as hagfish variable
lymphocyte receptor (VLR) fusions, are reported. These structures suggest that
the aspartate mutation does not generate any significant conformational change
in the protein, but instead leads to an altered interaction with partner
receptors.
|
|
|
|
|
|
|
