4oib: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4oib]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OIB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OIB FirstGlance]. <br> | <table><tr><td colspan='2'>[[4oib]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OIB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OIB FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oi9|4oi9]], [[4oia|4oia]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oi9|4oi9]], [[4oia|4oia]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oib OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oib RCSB], [http://www.ebi.ac.uk/pdbsum/4oib PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oib OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oib RCSB], [http://www.ebi.ac.uk/pdbsum/4oib PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/ICAM5_HUMAN ICAM5_HUMAN]] ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Barredo, R | [[Category: Barredo, R]] | ||
[[Category: Casasnovas, J M | [[Category: Casasnovas, J M]] | ||
[[Category: Ghamberg, C | [[Category: Ghamberg, C]] | ||
[[Category: Jimenez, D | [[Category: Jimenez, D]] | ||
[[Category: Recacha, R | [[Category: Recacha, R]] | ||
[[Category: Tian, L | [[Category: Tian, L]] | ||
[[Category: Cell adhesion]] | [[Category: Cell adhesion]] | ||
[[Category: Cell surface]] | [[Category: Cell surface]] | ||
Revision as of 05:38, 25 December 2014
Crystal Structure of ICAM-5 D1-D4 ectodomain fragment, Space Group R3Crystal Structure of ICAM-5 D1-D4 ectodomain fragment, Space Group R3
Structural highlights
Function[ICAM5_HUMAN] ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). Publication Abstract from PubMedIntercellular 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. Crystal structures of an ICAM-5 ectodomain fragment show electrostatic-based homophilic adhesions.,Recacha R, Jimenez D, Tian L, Barredo R, Gahmberg CG, Casasnovas JM Acta Crystallogr D Biol Crystallogr. 2014 Jul 1;70(Pt 7):1934-43. doi:, 10.1107/S1399004714009468. Epub 2014 Jun 29. PMID:25004970[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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