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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >A reassessment of the MAdCAM-1 structure and its role in integrin recognition.
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A reassessment of the MAdCAM-1 structure and its role in integrin recognition.

机译：MAdCAM-1结构及其的重新评估在整合素识别中的作用。

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摘要

Mucosal addressin cell-adhesion molecule (MAdCAM-1) is a membrane-bound leukocyte receptor regulating both the passage and retention of leukocytes in mucosal tissues. A crystal structure for the two extracellular amino-terminal domains of human MAdCAM-1 has previously been reported, confirming their expected immunoglobulin superfamily topology. In this study, a second crystal structure of this fragment is described. Although the overall structure is similar to that previously reported, one edge strand in the amino-terminal domain is instead located on the opposite sheet. This alters the arrangement and conformation of amino acids in this region that have previously been shown to be crucial for ligand binding. MAdCAM-1 is also seen to form dimers within the crystal lattice, raising the possibility that oligomerization may influence the biological role of this adhesion molecule.
机译：粘膜addressin酶分子(MAdCAM-1)是一种膜结合白细胞受体调节通道和保留白细胞在粘膜组织。两个细胞外结构人类MAdCAM-1伴域此前报道,确认他们预期免疫球蛋白超科拓扑。这项研究中,第二个晶体结构片段。结构类似于先前报道,伴域边缘链之一而不是位于相反的表。改变氨基酸的安排和构象以前的酸在这个地区配体结合的关键。也见过晶体内形成二聚体吗晶格,提高的可能性齐聚反应可能会影响生物的作用的粘附分子。

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