CRYSTAL-STRUCTURE OF RECOMBINANT HUMAN T-CELL CYCLOPHILIN-A AT 2.5-A RESOLUTION
CRYSTAL-STRUCTURE OF RECOMBINANT HUMAN T-CELL CYCLOPHILIN-A AT 2.5-A RESOLUTION
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DOI：
10.1073/pnas.88.21.9483
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发表时间：
1991-11-01
影响因子：
11.1
通讯作者：
WALSH, CT
中科院分区：
文献类型：
--
作者：
KE, HM;ZYDOWSKY, LD;WALSH, CT
未连接的人T细胞重组亲环蛋白的结构已通过多种同晶置换方法在3埃分辨率下测定，并在2.5埃分辨率下精制至R因子为0.209。键长和键角的均方根误差分别为0.013埃和2.8度，从理想的几何形状。整体结构是一个β-桶，由八个反平行的β-链缠绕在桶表面和两个α-螺旋坐在顶部和底部关闭桶。在桶内，七个芳香族和其他疏水残基形成一个紧凑的疏水核。一个由Lys-118至His-126的环和四条β链（B3-B6）组成的口袋，我们推测是环孢菌素A的结合位点。
The structure of the unligated human T-cell recombinant cyclophilin has been determined at 3 angstrom resolution by multiple isomorphous replacement methods and refined at 2.5 angstrom resolution to an R factor of 0.209. The root-mean-square errors of the bond lengths and bond angles are 0.013 angstrom and 2.8-degrees from ideal geometry, respectively. The overall structure is a beta-barrel, consisting of eight antiparallel beta-strands wrapping around the barrel surface and two alpha-helices sitting on the top and the bottom closing the barrel. Inside the barrel, seven aromatic and other hydrophobic residues form a compact hydrophobic core. A loop of Lys-118 to His-126 and four beta-strands (B3-B6) constitute a pocket we speculate to be the binding site of cyclosporin A.