Crystal structure of the BAFF-BAFFR complex and its implications for receptor activation, crystal structure of drosophila angiotensin I-converting enzyme bound to captopril and lisinoprilBAFF-BAFFR 결합체 구조연구, 초파리 angiotensin I-converting enzyme 단백질과 그 저해제의 상호작용 연구

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dc.contributor.advisorYoo, Ook-Joon-
dc.contributor.advisorLee, Jie-Oh-
dc.contributor.advisor유욱준-
dc.contributor.advisor이지오-
dc.contributor.authorKim, Ho-Min-
dc.contributor.author김호민-
dc.date.accessioned2011-12-12T07:54:34Z-
dc.date.available2011-12-12T07:54:34Z-
dc.date.issued2005-
dc.identifier.urihttp://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=249388&flag=dissertation-
dc.identifier.urihttp://hdl.handle.net/10203/27596-
dc.description학위논문(박사) - 한국과학기술원 : 생명과학과, 2005.8, [ 1책(면수복잡) ]-
dc.description.abstractBAFF (B-cell activating factor, also termed BLyS, TALL-1, THANK, and zTNF4) is a key regulator of B-lymphocyte maturation. BAFF has sequence and structural homology with TNF family proteins. Its biological role is mediated by the specific receptors BCMA, TACI, and BAFF-R. BAFF-R appears to be the major BAFF receptor for B-cell development in vivo. We have determined the crystal structure of BAFF-R bound to BAFF at a resolution of 3.3Å. The extracellular domain of human BAFF-R were co-expressed with human BAFF in Hi5 insect cells (Invitrogen) using a recombinant baculovirus system. The BAFF/BAFF-R complexes are purified and crystallized. The BAFF-R extracellular domain adopts a β -hairpin structure, and binds to the virus-like BAFF cage in a 1:1 molar ratio. The conserved DxL motif of BAFF-R is located on the tip of the β -turn, and plays an indispensable role in the binding of BAFF. The crystal structure shows that a unique dimeric interaction occurs between the BAFF-R monomers in the virus-like cage complex. Binding of BAFF-R to trimeric BAFF induces multimerization of the complex in solution. Both the cysteine-rich domains (CRDs) of TACI contain the DxL motifs and may simultaneously interact with the BAFF dimer in the virus-like cage. We propose that in the complex with the BAFF cage, the TACI intracellular domains are arranged differently from those of BAFF-R or BCMA.eng
dc.languageeng-
dc.publisher한국과학기술원-
dc.subjectBAFF-BAFFR-
dc.subjectangiotensin I-converting enzyme-
dc.subject단백질 결정구조-
dc.subjectBAFF-BAFFR-
dc.subjectCrystal structure-
dc.subjectangiotensin I-converting enzyme-
dc.titleCrystal structure of the BAFF-BAFFR complex and its implications for receptor activation, crystal structure of drosophila angiotensin I-converting enzyme bound to captopril and lisinopril-
dc.title.alternativeBAFF-BAFFR 결합체 구조연구, 초파리 angiotensin I-converting enzyme 단백질과 그 저해제의 상호작용 연구-
dc.typeThesis(Ph.D)-
dc.identifier.CNRN249388/325007 -
dc.description.department한국과학기술원 : 생명과학과, -
dc.identifier.uid020015094-
dc.contributor.localauthorYoo, Ook-Joon-
dc.contributor.localauthorLee, Jie-Oh-
dc.contributor.localauthor유욱준-
dc.contributor.localauthor이지오-
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