CRYSTALLIZATION, CRYSTAL-STRUCTURE ANALYSIS AND ATOMIC MODEL OF COMPLEX FORMED BY A HUMAN FC FRAGMENT AND FRAGMENT-B OF PROTEIN-A FROM STAPHYLOCOCCUS-AUREUS
CRYSTALLIZATION, CRYSTAL-STRUCTURE ANALYSIS AND ATOMIC MODEL OF COMPLEX FORMED BY A HUMAN FC FRAGMENT AND FRAGMENT-B OF PROTEIN-A FROM STAPHYLOCOCCUS-AUREUS
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DOI：
10.1515/bchm2.1978.359.2.975
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发表时间：
1978-01-01
影响因子：
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通讯作者：
SJOQUIST, J
中科院分区：
文献类型：
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作者：
DEISENHOFER, J;JONES, TA;SJOQUIST, J
制备了人Fc片段与金黄色葡萄球菌蛋白A片段B(FB)形成的复合体晶体，并通过多次同象置换高分辨率测定了其晶体结构。通过将这些相与FC组分的计算相结合，相态得到了显著改善。Fb是一种由3个平行螺旋组成的三角形排列的小球状蛋白质。它通过头两个螺旋与Fc结合，并连接到CH2和CH3的片段上。在络合物和FC碎片晶体中，CH3模块没有变化，但CH2相对于CH3的位置略有变化。CH2的上1/3在复杂的晶体中是无序的。讨论了这种紊乱的可能来源。
Crystals of the complex formed by human Fc fragment and fragment B (FB) of protein A from S. aureus were prepared and the crystal structure determined at high resolution by multiple isomorphous replacement. Phases were improved considerably by combining these phases with calculated phases from the Fc component. FB is a small globular protein built of 3 parallel helices arranged in a triangular array. It binds by the first 2 helices to Fc and is attached to segments of CH2 and CH3. The CH3 module is unchanged between complex and Fc fragment crystals, but CH2 changes its position slightly relative to CH3. The upper 1/3 of CH2 is disordered in the complex crystals. Possible sources of this disorder are discussed.