HIGH-RESOLUTION CRYSTAL-STRUCTURES AND COMPARISONS OF T-STATE DEOXYHEMOGLOBIN AND 2 LIGANDED T-STATE HEMOGLOBINS - T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN
HIGH-RESOLUTION CRYSTAL-STRUCTURES AND COMPARISONS OF T-STATE DEOXYHEMOGLOBIN AND 2 LIGANDED T-STATE HEMOGLOBINS - T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN
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DOI：
10.1016/0022-2836(92)90842-8
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发表时间：
1992-11-20
影响因子：
5.6
通讯作者：
DODSON, G
中科院分区：
文献类型：
--
作者：
LIDDINGTON, R;DEREWENDA, Z;DODSON, G
血红蛋白（Hb）中协同性的起源在于T状态的亲和力降低。从聚乙二醇生长的T-状态Hb晶体可以在分子不切换到R高亲和力状态的情况下配体化。T-态α-氧合血红蛋白和T-态甲硫氨酸血红蛋白的X射线分析确定了亲和力降低的结构基础。血红素环境中的化学张力的性质在α血红素和β血红素中是不同的。在T态的连接过程中，有一些小而明确的结构变化：这些变化被证明与T → R转变中发生的较大变化的方向基本相同。
The origin of co-operativity in haemoglobin (Hb) resides in the reduced affinity of the T-state. T-state Hb crystals grown from polyethyleneglycol can be liganded without the molecule switching to the R high affinity state. X-ray analysis of T-state α-oxy Hb and T-state met Hb has identified the structural basis for reduced affinity. The nature of the chemical tension at the haem environment is different in the α and β haems. There are small but definite structural changes associated with ligation in the T-state: these prove to be mostly in the same direction as the larger changes that occur in the T → R transition.