Structure of the SH3 domain of rat endophilin A2.
Structure of the SH3 domain of rat endophilin A2.
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DOI：
10.1107/s1744309108007574
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发表时间：
2008-04
期刊：
影响因子：
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通讯作者：
P. Loll;E. Swain;Yuan Chen;Brian T Turner;Ji-fang Zhang
中科院分区：
文献类型：
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作者：
P. Loll;E. Swain;Yuan Chen;Brian T Turner;Ji-fang Zhang
采用多波长异常色散法测定了大鼠亲内蛋白A2 SH3结构域的晶体结构，并在1.70 a到R的分辨率下进行了细化，R（自由）值分别为0.196和0.217。该结构遵循规范的sh3结构域折叠，与嗜内肽A1和A3的相应结构域高度相似。晶格中两个分子之间的分子间包装相互作用利用了在sh3结构域配体识别中常见的特征，包括将脯氨酸侧链插入蛋白质的配体结合槽中，以及由RT环上的一组酸性侧链识别碱性残基。
The crystal structure of the SH3 domain of rat endophilin A2 has been determined by the multiwavelength anomalous dispersion method and refined at a resolution of 1.70 A to R and R(free) values of 0.196 and 0.217, respectively. The structure adheres to the canonical SH3-domain fold and is highly similar to those of the corresponding domains of endophilins A1 and A3. An intermolecular packing interaction between two molecules in the lattice exploits features that are commonly observed in SH3-domain ligand recognition, including the insertion of a proline side chain into the ligand-binding groove of the protein and the recognition of a basic residue by a cluster of acidic side chains on the RT loop.