4OIA | pdb_00004oia

Crystal structures of an ICAM-5 ectodomain fragment show electrostatic-based homophilic adhesions.

(2014) Acta Crystallogr D Biol Crystallogr&nbsp70: 1934-1943

• PubMed:&nbsp25004970&nbspSearch on PubMedSearch on PubMed Central
• DOI:&nbsphttps://doi.org/10.1107/S1399004714009468
• Primary Citation of Related Structures: &nbsp
  4OI9, 4OIA, 4OIB


• PubMed Abstract:&nbsp
  

  Intercellular cell adhesion molecule-5 (ICAM-5) is a member of the ICAM subfamily that is exclusively expressed in the telencephalon region of the brain. The crystal structure of the four most N-terminal glycosylated domains (D1-D4) of ICAM-5 was determined in three different space groups and the D1-D5 fragment was modelled. The structures showed a curved molecule with two pronounced interdomain bends between D2 and D3 and between D3 and D4, as well as some interdomain flexibility. In contrast to ICAM-1, ICAM-5 has patches of positive and negative electrostatic charge at D1-D2 and at D3-D5, respectively. ICAM-5 can mediate homotypic interactions. In the crystals, several charge-based intermolecular interactions between the N-terminal and C-terminal moieties of the ICAM-5 molecules were observed, which defined an interacting surface in the D1-D4 fragment. One of the crystal lattices has a molecular assembly that could represent the homophilic ICAM-5 cell adhesion complex in neurons.

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Organizational Affiliation:&nbsp

Centro Nacional de Biotecnología (CNB-CSIC), Campus Universidad Autónoma de Madrid, Darwin 3,, 28049 Madrid, Spain.