6QM3

Crystal structure of a calcium- and sodium-bound mouse Olfactomedin-1 disulfide-linked dimer of the Olfactomedin domain and part of coiled coil

Summary for 6QM3

• Entry DOI: 10.2210/pdb6qm3/pdb
• Descriptor: Noelin, 2-acetamido-2-deoxy-beta-D-glucopyranose, CACODYLATE ION, ... (7 entities in total)
• Functional Keywords: calcium, beta-propeller, secreted, brain, signaling protein
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 2
• Total formula weight: 65750.80

Authors

Pronker, M.F.,van den Hoek, H.G.,Janssen, B.J.C. (deposition date: 2019-02-01, release date: 2019-09-11, Last modification date: 2024-11-06)

Primary citation

Pronker, M.F.,van den Hoek, H.,Janssen, B.J.C.
Design and structural characterisation of olfactomedin-1 variants as tools for functional studies.
BMC Mol Cell Biol, 20:50-50, 2019

PubMed Abstract: Olfactomedin-1 (Olfm1; also known as Noelin or Pancortin) is a highly-expressed secreted brain and retina protein and its four isoforms have different roles in nervous system development and function. Structural studies showed that the long Olfm1 isoform BMZ forms a disulfide-linked tetramer with a V-shaped architecture. The tips of the Olfm1 "V" each consist of two C-terminal β-propeller domains that enclose a calcium binding site. Functional characterisation of Olfm1 may be aided by new biochemical tools derived from these core structural elements.

PubMed: 31726976
DOI: 10.1186/s12860-019-0232-1

Experimental method

X-RAY DIFFRACTION (2 Å)