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Binding Mode Analysis of Bacillus subtilis Obg with Ribosomal Protein L13 using Macro-molecular Docking Study

등록일
2008년 2월 14일 10시 42분 26초
접수번호
1269
발표코드
31P57포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 <발표Ⅱ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
이윤호, 방우영, 이근우1
경상대학교 응용생명과학부,
1경상대학교 생화학과 응용생명과학부 EB-NCRC,
The bacterial Obg proteins belong to the subfamily of large GTPase proteins that contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain which has a unique Obg fold. Although functions of Obg proteins are not yet fully understood, it reveals the existence of a new pathway of replication controlled by the nucleotide pool and suggests unsuspected links between replication, proteins synthesis, and cellular differentiation. In addition, experimental results were revealed that Obg can specifically bind to ribosomal protein L13 in an affinity blot assay. Docking of Obg protein with ribosomal protein L13 was performed by Daughter of Turnip (DOT) 2.0 macro-molecular docking software and reasonable binding site was predicted. In this study we have focused the binding mode of Obg with L13.

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