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7LU6

Crystal structure of the mouse Kirrel3 D1 homodimer

Summary for 7LU6
Entry DOI10.2210/pdb7lu6/pdb
Related7LTW
DescriptorKin of IRRE-like protein 3, SODIUM ION (3 entities in total)
Functional Keywordsimmunoglobulin superfamily, cell surface receptor, nervous system, cell adhesion
Biological sourceMus musculus (Mouse)
Total number of polymer chains8
Total formula weight97421.78
Authors
Roman, C.A.,Pak, J.S.,Wang, J.,Ozkan, E. (deposition date: 2021-02-21, release date: 2021-11-24, Last modification date: 2024-10-23)
Primary citationWang, J.,Vaddadi, N.,Pak, J.S.,Park, Y.,Quilez, S.,Roman, C.A.,Dumontier, E.,Thornton, J.W.,Cloutier, J.F.,Ozkan, E.
Molecular and structural basis of olfactory sensory neuron axon coalescence by Kirrel receptors.
Cell Rep, 37:109940-109940, 2021
Cited by
PubMed Abstract: Projections from sensory neurons of olfactory systems coalesce into glomeruli in the brain. The Kirrel receptors are believed to homodimerize via their ectodomains and help separate sensory neuron axons into Kirrel2- or Kirrel3-expressing glomeruli. Here, we present the crystal structures of homodimeric Kirrel receptors and show that the closely related Kirrel2 and Kirrel3 have evolved specific sets of polar and hydrophobic interactions, respectively, disallowing heterodimerization while preserving homodimerization, likely resulting in proper segregation and coalescence of Kirrel-expressing axons into glomeruli. We show that the dimerization interface at the N-terminal immunoglobulin (IG) domains is necessary and sufficient to create homodimers and fail to find evidence for a secondary interaction site in Kirrel ectodomains. Furthermore, we show that abolishing dimerization of Kirrel3 in vivo leads to improper formation of glomeruli in the mouse accessory olfactory bulb as observed in Kirrel3 animals. Our results provide evidence for Kirrel3 homodimerization controlling axonal coalescence.
PubMed: 34731636
DOI: 10.1016/j.celrep.2021.109940
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

246031

数据于2025-12-10公开中

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