4ZG0: Crystal Structure Of Mouse Syndesmos Protein

Citation:
Abstract
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 alpha-helices and seven beta-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 alpha-helix 4, 7 and beta-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 muM) 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.
PDB ID: 4ZG0Download
MMDB ID: 139816
PDB Deposition Date: 2015/4/22
Updated in MMDB: 2016/06
Experimental Method:
x-ray diffraction
Resolution: 2.01  Å
Source Organism:
Similar Structures:
Biological Unit for 4ZG0: dimeric; determined by author and by software (PISA)
Molecular Components in 4ZG0
Label Count Molecule
Proteins (2 molecules)
2
Protein Syndesmos(Gene symbol: Nudt16l1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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