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Title: Crystal structure of syndesmos and its interaction with Syndecan-4 proteoglycan

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{sup 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{sup cyto} was characterized as a low-affinity interaction (K{sub d} = 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. - Highlights: • Crystal structure of syndesmos has been determined as a dimer at 2.01 Å resolution. • The molecular topologymore » of syndesmos resembles that of the Nudix hydrolase protein. • The structure of the Nudix motif of syndesmos is quite different from that of X29. • Syndesmos binds cytoplasmic domain of syndecan-4 proteoglycan with low affinity.« less
Authors:
 [1] ;  [2] ;  [1] ;  [2] ;  [2] ;  [1]
  1. Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul, 120-749 (Korea, Republic of)
  2. Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul, 120-749 (Korea, Republic of)
Publication Date:
OSTI Identifier:
22462145
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 463; Journal Issue: 4; Other Information: Copyright (c) 2015 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ADHESION; AFFINITY; CONTROL; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DIMERS; INTERFACES; NMR SPECTRA; NUCLEAR MAGNETIC RESONANCE; NUCLEOSIDES; PHOSPHATES; PROTEINS; SIGNALS; SURFACES; TOPOLOGY; X RADIATION