4oi9: Difference between revisions
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<StructureSection load='4oi9' size='340' side='right'caption='[[4oi9]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='4oi9' size='340' side='right'caption='[[4oi9]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4oi9]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4oi9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OI9 FirstGlance]. <br> | ||
</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4oi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oi9 OCA], [https://pdbe.org/4oi9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oi9 RCSB], [https://www.ebi.ac.uk/pdbsum/4oi9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oi9 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://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: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Barredo | [[Category: Barredo R]] | ||
[[Category: Casasnovas | [[Category: Casasnovas JM]] | ||
[[Category: Ghamberg | [[Category: Ghamberg C]] | ||
[[Category: Jimenez | [[Category: Jimenez D]] | ||
[[Category: Recacha | [[Category: Recacha R]] | ||
[[Category: Tian | [[Category: Tian L]] | ||
Latest revision as of 06:22, 21 November 2024
Crystal Structure of ICAM-5 D1-D4 ectodomain fragment, Space Group P21Crystal Structure of ICAM-5 D1-D4 ectodomain fragment, Space Group P21
Structural highlights
FunctionICAM5_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. See AlsoReferences
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