CRYSTAL-STRUCTURE OF THE A-DOMAIN FROM THE A-SUBUNIT OF INTEGRIN CR3 (CD11B/CD18)
CRYSTAL-STRUCTURE OF THE A-DOMAIN FROM THE A-SUBUNIT OF INTEGRIN CR3 (CD11B/CD18)
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DOI：
10.1016/0092-8674(95)90517-0
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发表时间：
1995-02-24
期刊：
影响因子：
64.5
通讯作者：
LIDDINGTON, R
中科院分区：
文献类型：
--
作者：
LEE, JO;RIEU, P;LIDDINGTON, R
我们已经从整合素 CR3 的 a 链中确定了 A 结构域的高分辨率晶体结构。该结构域采用经典的 α/β“罗斯曼”折叠，并在其表面包含不寻常的 Mg2+ 配位位点。其中一个配位配体是来自另一个 A 结构域分子的谷氨酸侧链。我们认为该位点代表了用于结合蛋白配体的一般金属离子依赖性粘附位点（MIDAS）。我们进一步提出整联蛋白的β亚基在修饰的A结构域内包含MIDAS基序。我们的晶体结构将允许为 A 结构域超家族的其他成员建立可靠的模型，并应促进新型粘附调节药物的开发。
We have determined the high resolution crystal structure of the A domain from the a chain of integrin CR3. The domain adopts a classic alpha/beta ''Rossmann'' fold and contains an unusual Mg2+ coordination site at its surface. One of the coordinating ligands is the glutamate side chain from another A domain molecule. We suggest that this site represents a general metal ion-dependent adhesion site (MIDAS) for binding protein ligands. We further propose that the beta subunits of integrins contain a MIDAS motif within a modified A domain. Our crystal structure will allow reliable models to be built for other members of the A domain superfamily and should facilitate development of novel adhesion modulatory drugs.