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The Structure of Physarum polycephalum hemagglutinin I suggests a minimal carbohydrate recognition domain of legume lectin fold.

Abstract：

:Physarum polycephalum hemagglutinin I (HA1) is a 104-residue protein that is secreted to extracellular space. The crystal structure of HA1 has a β-sandwich fold found among lectin structures, such as legume lectins and galectins. Interestingly, the β-sandwich of HA1 lacks a jelly roll motif and is essentially composed of two simple up-and-down β-sheets. This up-and-down β-sheet motif is well conserved in other legume lectin-like proteins derived from animals, plants, bacteria, and viruses. It is more noteworthy that the up-and-down β-sheet motif includes many residues that make contact with the target carbohydrates. Our NMR data demonstrate that HA1 lacking a jelly roll motif also binds to its target glycopeptide. Taken together, these data show that the up-and-down β-sheet motif provides a fundamental scaffold for the binding of legume lectin-like proteins to the target carbohydrates, and the structure of HA1 suggests a minimal carbohydrate recognition domain.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Kouno T,Watanabe N,Sakai N,Nakamura T,Nabeshima Y,Morita M,Mizuguchi M,Aizawa T,Demura M,Imanaka T,Tanaka I,Kawano K

doi

10.1016/j.jmb.2010.11.024

subject

Has Abstract

pub_date

2011-01-14 00:00:00

pages

560-9

issue

2

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(10)01254-4

journal_volume

405

pub_type

杂志文章

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