투고논문
| JKMRS Volume 19, No 2, pp 88-94;Structural stability of CD1 do... | |
|---|---|
| 2015년 10월 13일 / 조회수: 623 | |
|
Structural stability of CD1 domain of
human mitotic checkpoint serine/threonine-protein kinase, Bub1 Hyun-Hwi Kim1,
Hyun-Kyu Song2, Bong-Jin Lee3*, and Sung Jean Park1* 1 College of Pharmacy,
Gachon University, 534-2 Yeonsu-dong, Yeonsu-gu, Incheon, Republic of Korea 2School of Life Sciences
and Biotechnology, Korea University, Anam-Dong, Seongbuk-Gu, Seoul 136-701,
Korea 3Research Institute of
Pharmaceutical Sciences, College of Pharmacy, Seoul National University, San
56-1, Shillim-Dong, Kwanak-Gu, Seoul 151-742, Korea Received Aug 16, 2015; Revised
Sep 12, 2015; Accepted Sep 20, 2015 Abstract Bub1
is one of the spindle checkpoint proteins and plays a role in recruitment of
the related proteins to kinetochore. Here, we studied the structural characteristic
of the evolutionarily conserved 160 amino acid region in the N-terminus (hBub1
CD1), using Circular Dichroism (CD) and NMR. Our CD results showed that hBub1
CD1 is a highly helical protein and its structure was affected by pH: as pH was
elevated to basic pH, the helical propensity increased. This could be related
to the surface charge of the hBub1 CD1. However, the structural change did not
largely depend on the salt concentration, though the thermal stability a little
increased. The previous NMR analysis1 revealed that the
hBub1 CD1 adopts eight helices, which is consistent with the CD result. Our
result would be helpful for evaluating the molecular mechanism of the hBub1 CD1
and protein-protein interactions. Keywords NMR, CD, Bub1, human mitotic checkpoint
serine/threonine-protein kinase |
|
| 첨부파일 | 6_박성진.pdf |