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PDBsum entry 4zg0
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References listed in PDB file
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Key reference
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Title
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Crystal structure of syndesmos and its interaction with syndecan-4 proteoglycan.
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Authors
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H.Kim,
J.Yoo,
I.Lee,
Y.J.Kang,
H.S.Cho,
W.Lee.
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Ref.
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Biochem Biophys Res Commun, 2015,
463,
762-767.
[DOI no: ]
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PubMed id
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Abstract
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Syndesmos, nucleoside diphosphate linked moiety X (nudix)-type motif 16-like 1
(Nudt16l1), is evolutionarily divergent from the Nudt16 family. Syndesmos, which
is co-localized with syndecan-4 cytoplasmic domain (Syn4(cyto)) in focal
contacts, interacts with various cell adhesion adaptor proteins to control cell
signaling. We determined the X-ray crystal structure of syndesmos; it is
composed of seven α-helices and seven β-strands. Although syndesmos has a
molecular topology similar to that of nudix hydrolase proteins, the structure of
the nudix motif differs from that of X29. The dimeric interface of syndesmos is
composed of α-helix 4, 7 and β-strand 2, 7, which primarily form hydrophobic
interactions. The binding interaction between syndesmos and syn4(cyto) was
characterized as a low-affinity interaction (Kd = 62 μM) by surface plasmon
resonance (SPR) and nuclear magnetic resonance (NMR). The NMR resonances of Lys
(177, 178, 179), Gly182, and Ser183 in the C1 region and Lys193 and Lys194 in
the V region of syndecan-4 are perturbed upon syndesmos binding. Our results
provide structural insight into the molecular function of syndesmos in the
regulation of cell signaling via binding to syndecan-4.
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