RAD52-RPA Interactions (literature search)
Summary References Sequence Structure
|
RPA residues |
RAD52 binding site |
Specific Reference |
|
RPA34C (last 33 aa) |
RAD52 (221-280) |
Park (Aug. ’96) |
|
RPA32C (172-270) |
RAD52 (257-274) |
Bochkareva (Oct. ’00) |
|
RPA32C (224-271) |
RAD52 (218-303) |
Borgstahl (Aug. ’02) |
|
RPA70 (169-326) |
RAD52 (218-303) |
Borgstahl (Aug. ’02) |
A. Information on specific
interaction sites
RPA34C (last 33 aa) interacts with amino acids 221-280 in RAD52.
RPA34 has higher affinity to RAD52 than RPA70 and RPA14 has none.
hRAD52 (221-280) has only 7% homology in other species. (TOP)
RAD52 interacts with all 3 subunits of yeast RPA.
RAD52 interaction with yeast RPA70 > yRPA32 > yRPA14.
This interaction might be between yRPA70 and DNA binding domain of RAD52.
yRPA70 interacts with RAD52 but not with RAD51, RAD55 and RAD57. (TOP)
RPA32C (172-270) interacts with RAD52 (257-274).
(Same paper is detailed in XPA page). (TOP)
RAD52 (218-303) binds either RPA32C (224-271) or RPA70 (169-326). (TOP)
Park et al. paper listed above is referred. (TOP)
Formation of RPA-RAD52-RAD59 complex suggested. (TOP)
B. General interaction
information
Source: AAS00097 – hRAD52 on NCBI protein sequence database [gi: 41324138].
1 MSGTEEAILG GRDSHPAAGG GSVLCFGQCQ YTAEEYQAIQ
KALRQRLGPE YISSRMAGGG
61 QKVCYIEGHR VINLANEMFG YNGWAHSITQ QNVDFVDLNN
GKFYVGVCAF VRVQLKDGSY
121 HEDVGYGVSE
GLKSKALSLE KARKEAVTDG LKRALRSFGN ALGNCILDKD YLRSLNKLPR
181 QLPLEVDLTK
AKRQDLEPSV EEARYNSCRP NMALGHPQLQ QVTSPSRPSH AVIPADQDCS
241 SRSLSSSAVE
SEATHQRKLR QKQLQQQFRE RMEKQQVRVS TPSAEKSEAA PPAPPVTHST
301 PVTVSEPLLE
KDFLAGVTQE LIKTLEDNSE KWAVTPDAGD GVVKPSSRAD PAQTSDTLAL
361 NNQMVTQNRT PHSVCHQKPQ AKSGSWDLQT YSADQRTTGN WESHRKSQDM
KKRKYDPS
RAD52
interacts with RPA32C and RPA70(169-326) domains,
whose tertiary structures have been determined.
Please
click on the links below to view the domains:
1.
RPA32C – Figure obtained through VMD. (or check 1DPU
in PDB)
2.
RPA70(181-432)
– Figure obtained through VMD.
(or check 1FGU
in PDB)