Structural mechanism of the antigen recognition by the L1 cell adhesion molecule antibody A10-A3
DC Field | Value | Language |
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dc.contributor.author | Wei, Chun Hua | - |
dc.contributor.author | Lee, Eung Suk | - |
dc.contributor.author | Jeon, Jeong Yi | - |
dc.contributor.author | Heo, Yong-Seok | - |
dc.contributor.author | Kim, Seung Jun | - |
dc.contributor.author | Jeon, Young Ho | - |
dc.contributor.author | Kim, Kyung Hyun | - |
dc.contributor.author | Hong, Hyo Jeong | - |
dc.contributor.author | Ryu, Seong Eon | - |
dc.date.accessioned | 2022-07-16T22:24:05Z | - |
dc.date.available | 2022-07-16T22:24:05Z | - |
dc.date.created | 2021-05-12 | - |
dc.date.issued | 2011-01 | - |
dc.identifier.issn | 0014-5793 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/169298 | - |
dc.description.abstract | The L1CAM antibody A10-A3 efficiently reduces tumor growth in a nude mouse model. Here, we describe the crystal structure of the Fab fragment of A10-A3 determined at 2.0 angstrom resolution. The A10-A3 antibody H3 loop reveals a characteristic arrangement of exposed aromatic residues that may play an important role in antigen binding. A structure model of the complex between L1CAM Ig1-4 and A10-A3 Fab indicates that the Fab binds to three small loops outside Ig1 and a residue between Ig1 and Ig2, consistent with an epitope mapping result. The data presented here should contribute to the design of high-affinity antibody for therapeutic purposes as well as to the understanding of neural cell remodeling and cancer progression mechanism mediated by L1CAM. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | WILEY | - |
dc.title | Structural mechanism of the antigen recognition by the L1 cell adhesion molecule antibody A10-A3 | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Ryu, Seong Eon | - |
dc.identifier.doi | 10.1016/j.febslet.2010.11.028 | - |
dc.identifier.scopusid | 2-s2.0-78650874809 | - |
dc.identifier.wosid | 000285921500026 | - |
dc.identifier.bibliographicCitation | FEBS LETTERS, v.585, no.1, pp.153 - 158 | - |
dc.relation.isPartOf | FEBS LETTERS | - |
dc.citation.title | FEBS LETTERS | - |
dc.citation.volume | 585 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 153 | - |
dc.citation.endPage | 158 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalResearchArea | Cell Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | GROWTH | - |
dc.subject.keywordPlus | IMMUNOGLOBULINS | - |
dc.subject.keywordPlus | INHIBITION | - |
dc.subject.keywordPlus | SUGGESTS | - |
dc.subject.keywordPlus | SYSTEM | - |
dc.subject.keywordPlus | FAMILY | - |
dc.subject.keywordPlus | CANCER | - |
dc.subject.keywordPlus | MODEL | - |
dc.subject.keywordAuthor | Crystal structure | - |
dc.subject.keywordAuthor | Antibody | - |
dc.subject.keywordAuthor | A10-A3 | - |
dc.subject.keywordAuthor | L1CAM | - |
dc.subject.keywordAuthor | Cancer | - |
dc.identifier.url | https://febs.onlinelibrary.wiley.com/doi/full/10.1016/j.febslet.2010.11.028 | - |
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