STRUCTURAL BASIS OF COOPERATIVITY OF ASPARTATE RECEPTOR

天冬氨酸受体是一种与天冬氨酸结合的二聚体受体。 负协作性。的周质结构域的结构 天冬氨酸受体，每个二聚体结合0、1和2个天冬氨酸 已经被X射线结晶学解决了。对晶体的检查 结构表明，天冬氨酸的两个结合部位是 一开始是一样的。在第一个天冬氨酸结合后， 是一种构象上的变化，使空地更加拥挤 因此不容易与第二天冬氨酸结合。一直以来 证明Ser68是变构转换所必需的 天冬氨酸受体的作用机制。比较这两个词的结构 野生型受体和68位残基的突变将揭示 变构相互作用的一般机制。

Aspartate receptor is a dimeric receptor that binds aspartate with negative cooperativity. The structures of the periplasmic domain of aspartate receptor with zero, one and two aspartates bound per dimer have been solved by x-ray crystallography. Examination of the crystal structures shows that the two binding sites for aspartate are initially identical. Upon the binding of the first aspartate, there is a change in conformation that makes the empty site more crowded and hence less easy to the binding of the second aspartate. It has been demonstrated that Ser68 is integral to the allosteric switching mechanism in the aspartate receptor. Comparing the structures of the wild-type receptor and mutations at the 68 residue would shed light on the general mechanism of allosteric interactions.