2008年度生化与细胞所学术年会通知
来源：
时间：2008-11-18
为了总结2008年的科研工作，展示各研究组的科研成果，加强研究组间的学术交流与合作，促进研究所整体科研水平的提高，我所将于2009年1月4 - 6日（地点另行通知）召开2008年度学术年会，会期3天。现将有关事项通知如下：
1．年会将安排大会特邀报告、研究组长学术报告、研究生学术报告、墙报交流等活动，同时将评选优秀研究生学术报告和学术墙报。
2．本次年会的学术报告（PI报告和研究生报告）由重点实验室推荐产生，根据会期暂定PI报告8-10人；学生报告12-15人。
3．每个研究组至少展出一份墙报。墙报按统一规格制作：110厘米（高）×80厘米（宽）。
4．年会将编印学术报告摘要和墙报摘要，请报告人和研究组尽快撰写有关摘要(“word”文本,英文撰写，格式附后)，并于12月15日前将摘要传至科研处吴雯英 (
wywu@sibs.ac.cn)。
5．每个研究组参加年会人数一般不超过5人（含PI和学生）。各研究组负责人、各中心平台负责人、所聘顾问的会务费由研究所承担；其他人员的与会费用(约650 元左右)由研究组承担。
生化与细胞所科研处
2008年11月18日
备注：
1. 大会特邀报告30分钟，提问15分钟；PI学术报告20分钟，提问15分钟；
研究生报告10分钟，提问10分钟。
2．墙报请按统一规格制作：110公分（高）×80公分（宽）
附：摘要样稿
Solution Structures of Ubiquitin-Binding Domains and their Binding Specificities with Ubiquitin
Aixin Song, Chenjie Zhou, Ziren Zhou, Jing Hong, Yonggang Chang,
Hongchang Gao, Donghai Lin, and Hongyu Hu
Ubiquitin (Ub) is a very important cellular signal that targets proteins for degradation or regulates their functions. Many proteins or domains are involved in this particular post-translational modification system. To understand the binding specificities of these small domains with Ub, which are vital to selection and regulation for diverse cellular processes, we determined several Ub-binding domains (UBD) derived from diverse Ub-related proteins, and investigated their binding specificities with Ub by NMR. These domains include ubiquitin-interacting motifs (UIM) from ataxin-3 (AT3-UIMs) and co-chaperone HSJ1a, and ubiquitin-associated domains (UBA) from BMSC-UbP (BMSC-UBA), E3 ligases c-Cbl (cUBA) and Cbl-b (UBAb).
The solution structure of AT3-UIMs includes two helices and a turn in the linker region. NMR titration revealed that both the motifs in the tandem UIMs can interact through the conserved residues with the Leu8-Ile44-Val70 hydrophobic patch of Ub. The single UIM1 and UIM2 of AT3 can also bind Ub, respectively, but with lower affinities. These results imply that interaction of the tandem UIMs with Ub may undergo with a cooperative manner between these two UIMs, suggesting that the cooperative interaction may have significant effect on the aggregation of polyglutamine tract in AT3 adjacent to the tandem UIMs.
All the three UBA domains having studied primarily consist of three a-helices with a hydrophobic patch. Chemical shift perturbation study revealed that the UBA domains bind with the conserved five-stranded b-sheet of Ub via hydrophobic interactions, except for cUBA that binds Ub very weakly. The hydrophobic surface distributions on the first helix play crucial roles in their differential affinities for Ub binding. The structural model of the BMSC-UBA domain complexed with Ub was constructed by chemical shift mapping combined with the program HADDOCK and confirmed by mutagenesis. This complex structure may provide structural insights into the interaction between UBA domains of Ub-associated proteins and Ub-like domains.
