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6QHJ

High-resolution crystal structure of calcium- and sodium-bound mouse Olfactomedin-1 beta-propeller domain

Summary for 6QHJ
Entry DOI10.2210/pdb6qhj/pdb
DescriptorNoelin, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (6 entities in total)
Functional Keywordscalcium, beta-propeller, secreted, brain, signaling protein
Biological sourceHomo sapiens (Human)
Total number of polymer chains1
Total formula weight31313.62
Authors
Pronker, M.F.,van den Hoek, H.G.,Janssen, B.J.C. (deposition date: 2019-01-16, release date: 2019-09-11, Last modification date: 2024-11-20)
Primary citationPronker, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.25 Å)
Structure validation

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