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3eob
From Proteopedia
(Difference between revisions)
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==Crystal structure the Fab fragment of Efalizumab in complex with LFA-1 I domain, Form II== | ==Crystal structure the Fab fragment of Efalizumab in complex with LFA-1 I domain, Form II== | ||
| - | <StructureSection load='3eob' size='340' side='right' caption='[[3eob]], [[Resolution|resolution]] 3.60Å' scene=''> | + | <StructureSection load='3eob' size='340' side='right'caption='[[3eob]], [[Resolution|resolution]] 3.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3eob]] is a 6 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3eob]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EOB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3eo9|3eo9]], [[3eoa|3eoa]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3eo9|3eo9]], [[3eoa|3eoa]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IGG1 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IGG1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), LFA-1 I domain ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3eob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eob OCA], [https://pdbe.org/3eob PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eob RCSB], [https://www.ebi.ac.uk/pdbsum/3eob PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eob ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/ITAL_HUMAN ITAL_HUMAN]] Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. It is involved in a variety of immune phenomena including leukocyte-endothelial cell interaction, cytotoxic T-cell mediated killing, and antibody dependent killing by granulocytes and monocytes. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
| - | *[[Integrin|Integrin]] | + | *[[Integrin 3D structures|Integrin 3D structures]] |
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]] | *[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]] | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Ding, J]] | [[Category: Ding, J]] | ||
[[Category: Li, S]] | [[Category: Li, S]] | ||
Current revision
Crystal structure the Fab fragment of Efalizumab in complex with LFA-1 I domain, Form II
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Categories: Human | Large Structures | Ding, J | Li, S | Alternative splicing | Antibody | Calcium | Cd11a | Cell adhesion | Efalizumab | Fab | Glycoprotein | I domain | Immune system-cell adhesion complex | Integrin | Lfa-1 | Magnesium | Membrane | Polymorphism | Receptor | Transmembrane

