X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-A resolution.

X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-A resolution.
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DOI:
10.2210/pdb1a3k/pdb
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发表时间:
1998
期刊:
The Journal of biological chemistry
影响因子:
--
通讯作者:
J. Seetharaman;A. Kanigsberg;R. Slaaby;H. Leffler;S. Barondes;J. Rini
J. Seetharaman;A. Kanigsberg;R. Slaaby;H. Leffler;S. Barondes;J. Rini
中科院分区:
其他
文献类型:
--
作者:
J. Seetharaman;A. Kanigsberg;R. Slaaby;H. Leffler;S. Barondes;J. Rini

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半乳糖凝集素是具有相似的碳水化合物识别结构域(CRD)和对小β-半乳糖苷的亲和力的凝集素家族,但其对更复杂的糖缀合物的结合特异性显示出显著差异。我们在这里报告的X-射线晶体结构的人半乳糖凝集素-3 CRD,在复杂的乳糖和N-乙酰乳糖胺,在2.1-A的分辨率。该结构代表了从半乳糖凝集素确定的CRD的第一个例子,其不显示典型的2倍对称二聚体组织。与半乳糖凝集素-1和-2的已发表结构的比较提供了半乳糖凝集素-3所示的碳水化合物结合特异性差异的解释,以及它不能通过类似的CRD-CRD相互作用形成二聚体的事实。
Galectins are a family of lectins which share similar carbohydrate recognition domains (CRDs) and affinity for small beta-galactosides, but which show significant differences in binding specificity for more complex glycoconjugates. We report here the x-ray crystal structure of the human galectin-3 CRD, in complex with lactose and N-acetyllactosamine, at 2.1-A resolution. This structure represents the first example of a CRD determined from a galectin which does not show the canonical 2-fold symmetric dimer organization. Comparison with the published structures of galectins-1 and -2 provides an explanation for the differences in carbohydrate-binding specificity shown by galectin-3, and for the fact that it fails to form dimers by analogous CRD-CRD interactions.