4OI9
Crystal Structure of ICAM-5 D1-D4 ectodomain fragment, Space Group P21
Summary for 4OI9
| Entry DOI | 10.2210/pdb4oi9/pdb |
| Related | 4OIA 4OIB |
| Descriptor | Intercellular adhesion molecule 5, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | cell adhesion, cell surface, neurons, immunoglobulin superfamily, intercellular adhesion molecules, icam-5, telencephalin |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane; Single-pass type I membrane protein: Q9UMF0 |
| Total number of polymer chains | 1 |
| Total formula weight | 46363.69 |
| Authors | Recacha, R.,Jimenez, D.,Tian, L.,Barredo, R.,Ghamberg, C.,Casasnovas, J.M. (deposition date: 2014-01-19, release date: 2014-07-16, Last modification date: 2020-07-29) |
| Primary citation | Recacha, R.,Jimenez, D.,Tian, L.,Barredo, R.,Gahmberg, C.G.,Casasnovas, J.M. Crystal structures of an ICAM-5 ectodomain fragment show electrostatic-based homophilic adhesions. Acta Crystallogr.,Sect.D, 70:1934-1943, 2014 Cited by PubMed Abstract: 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. PubMed: 25004970DOI: 10.1107/S1399004714009468 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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