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제109회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Structure and Backbone Dynamics Studies of PRL-3: Comparison of the 15N NMR Relaxation Profiles of apo- and holo-PRL-3

등록일
2012년 2월 23일 10시 31분 59초
접수번호
1392
발표코드
PHYS.P-510 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
4월 25일 (수요일) 18:00~21:00
발표형식
포스터
발표분야
물리화학
저자 및
공동저자
강동일, 정기웅1, 김진경1, 김양미1
건국대학교 화학과, Korea
1건국대학교 생명공학과, Korea
Phosphatases of regenerating liver (PRL) constitute a novel class of small, prenylated phosphatases with oncogenic activity. In particular, PRL-3 is important in cancer metastasis. With the aim of verifying the functional importance of the inherent structural flexibility of PRL-3, we have investigated the structures and the dynamic properties of apo- and holo-PRL-3 using NMR spectroscopy. Structures of apo- and holo-PRL-3 showed substantial differences in the general acid loop. Cys104, Arg110, and Asp72, participating in the enzymatic reaction, are close with each other and induced closed conformation in holo-PRL-3. When orthovanadate is added to the apo-PRL-3, the NMR signals from the residues in the active site appeared, indicating that the conformation of this region has been stabilized. Ligand binding caused a large conformational rearrangement, influencing on the motional behavior of the loops near the active site. Model-free analysis showed that flexibility of general acid loop is increased while the flexibility of P-loop is decreased upon binding of vanadate ion. Also, Glu82 at α3 helix showed increase of flexibility and conformation exchange upon vanadate binding. These results imply that general acid loop and α5-α6 as well as P-loop is important in ligand recognition and the difference between the flexibilities of the loops in apo- and holo-PRL-3 controls the protein-ligand interaction.

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