DC Field | Value | Language |
---|---|---|
dc.contributor.advisor | Yoo, Ook-Joon | - |
dc.contributor.advisor | Lee, Jie-Oh | - |
dc.contributor.advisor | 유욱준 | - |
dc.contributor.advisor | 이지오 | - |
dc.contributor.author | Kim, Ho-Min | - |
dc.contributor.author | 김호민 | - |
dc.date.accessioned | 2011-12-12T07:54:34Z | - |
dc.date.available | 2011-12-12T07:54:34Z | - |
dc.date.issued | 2005 | - |
dc.identifier.uri | http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=249388&flag=dissertation | - |
dc.identifier.uri | http://hdl.handle.net/10203/27596 | - |
dc.description | 학위논문(박사) - 한국과학기술원 : 생명과학과, 2005.8, [ 1책(면수복잡) ] | - |
dc.description.abstract | BAFF (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.language | eng | - |
dc.publisher | 한국과학기술원 | - |
dc.subject | BAFF-BAFFR | - |
dc.subject | angiotensin I-converting enzyme | - |
dc.subject | 단백질 결정구조 | - |
dc.subject | BAFF-BAFFR | - |
dc.subject | Crystal structure | - |
dc.subject | angiotensin I-converting enzyme | - |
dc.title | 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 lisinopril | - |
dc.title.alternative | BAFF-BAFFR 결합체 구조연구, 초파리 angiotensin I-converting enzyme 단백질과 그 저해제의 상호작용 연구 | - |
dc.type | Thesis(Ph.D) | - |
dc.identifier.CNRN | 249388/325007 | - |
dc.description.department | 한국과학기술원 : 생명과학과, | - |
dc.identifier.uid | 020015094 | - |
dc.contributor.localauthor | Yoo, Ook-Joon | - |
dc.contributor.localauthor | Lee, Jie-Oh | - |
dc.contributor.localauthor | 유욱준 | - |
dc.contributor.localauthor | 이지오 | - |
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