%0 Journal Article
%T Homology model of NR2B and its binding with Con-G<br>NR2B的同源模建及其与Con-G的对接(英文)
%A CHEN Xiang
%A XU Jie-qiong
%A QIAN Ling-ling
%A ZHOU Wan-ling
%A ZHU Yong-ping
%A <br>陈翔
%A 许洁琼
%A 钱玲玲
%A 周晚玲
%A 朱永平
%J 浙江大学学报(农业与生命科学版)
%D 2010
%I Zhejiang University Press
%X A better understanding of the molecular determinants of agonist or antagonist selectivity and efficacy at the NMDA receptor is of both mechanistic and medical interest,and it might facilitate the design of therapeutically applicable compounds.In this work,homology model NR2B subunits of the NMDA receptor was constructed using three structural templates for the model building.This subunit model with the lowest energy was then assessed for the stereochemical quality and side chain environment.Conantokin-G (Con-G) was docked into the model allowing further validation of the active site architecture.In docking studies,the helical conformation of Con-G found in the solution was maintained in the bound state,and its structure was nicely fitted into the agonist binding cleft on the NR2B subunit.Structurally and functionally important residues were identified,including E2,Gla4,L5,Q9,I12 and Q13 of Con-G,and they interacted with E420,S421,D423,K458 and D715 of NR2B.Several H-bonds were also found.This model is consistent with most of the previous experiments,and should be useful for predicting binding interactions of newly designed NMDA receptor ligands.It may provide important clues in the discovery of useful NMDA receptor agonists and antagonists.
%K NR2B
%K Con-G(conantokin-G)
%K NR2B
%K Con-G (conantokin-G)
%K homology model
%K docking<br>同源模建
%K 对接
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=03F54A49DE00578AA0E5DDF5BC021AA7&cid=298920A27C9BAA22346FCA384240FAA4&jid=466C05D88593309B3EB5CF34361E6426&aid=66C01EAC0B062191EC3965181526EC6D&yid=140ECF96957D60B2&vid=933658645952ED9F&iid=E158A972A605785F&sid=26AEEED215BE97D0&eid=FA3423FC1AE95C4E&journal_id=1008-9209&journal_name=浙江大学学报(农业与生命科学版)&referenced_num=0&reference_num=34