3eoa

From Proteopedia

(Difference between revisions)

Revision as of 21:34, 2 December 2018

Crystal structure the Fab fragment of Efalizumab in complex with LFA-1 I domain, Form I

Structural highlights

3eoa is a 6 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3eo9, 3eob
Gene:	IGG1 (HUMAN), ITGAL, CD11A (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Lymphocyte function-associated antigen 1 (LFA-1) plays important roles in immune cell adhesion, trafficking, and activation and is a therapeutic target for the treatment of multiple autoimmune diseases. Efalizumab is one of the most efficacious antibody drugs for treating psoriasis, a very common skin disease, through inhibition of the binding of LFA-1 to the ligand intercellular adhesion molecule 1 (ICAM-1). We report here the crystal structures of the Efalizumab Fab alone and in complex with the LFA-1 alpha(L) I domain, which reveal the molecular mechanism of inhibition of LFA-1 by Efalizumab. The Fab binds with an epitope on the inserted (I) domain that is distinct from the ligand-binding site. Efalizumab binding blocks the binding of LFA-1 to ICAM-1 via steric hindrance between its light chain and ICAM-1 domain 2 and thus inhibits the activities of LFA-1. These results have important implications for the development of improved antibodies and new therapeutic strategies for the treatment of autoimmune diseases.

Efalizumab binding to the LFA-1 alphaL I domain blocks ICAM-1 binding via steric hindrance.,Li S, Wang H, Peng B, Zhang M, Zhang D, Hou S, Guo Y, Ding J Proc Natl Acad Sci U S A. 2009 Mar 17;106(11):4349-54. Epub 2009 Mar 3. PMID:19258452^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Li S, Wang H, Peng B, Zhang M, Zhang D, Hou S, Guo Y, Ding J. Efalizumab binding to the LFA-1 alphaL I domain blocks ICAM-1 binding via steric hindrance. Proc Natl Acad Sci U S A. 2009 Mar 17;106(11):4349-54. Epub 2009 Mar 3. PMID:19258452

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3eoa"

@@ Line 1: / Line 1: @@
 ==Crystal structure the Fab fragment of Efalizumab in complex with LFA-1 I domain, Form I==
 <StructureSection load='3eoa' size='340' side='right' caption='[[3eoa]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3eo9|3eo9]], [[3eob|3eob]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IGG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), ITGAL, CD11A ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3eoa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eoa OCA], [http://pdbe.org/3eoa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3eoa RCSB], [http://www.ebi.ac.uk/pdbsum/3eoa 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=3eoa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eoa OCA], [http://pdbe.org/3eoa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3eoa RCSB], [http://www.ebi.ac.uk/pdbsum/3eoa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3eoa ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eo/3eoa_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eo/3eoa_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 31: / Line 32: @@
 ==See Also==
 *[[Integrin|Integrin]]
-*[[Monoclonal Antibody|Monoclonal Antibody]]
+*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
 == References ==
 <references/>
@@ Line 39: / Line 40: @@
 [[Category: Ding, J]]
 [[Category: Li, S]]
+[[Category: Alternative splicing]]
 [[Category: Antibody]]
+[[Category: Calcium]]
 [[Category: Cd11a]]
 [[Category: Efalizumab]]
@@ Line 50: / Line 53: @@
 [[Category: Magnesium]]
 [[Category: Membrane]]
+[[Category: Polymorphism]]
 [[Category: Receptor]]
 [[Category: Transmembrane]]

3eoa

From Proteopedia

Revision as of 21:34, 2 December 2018

Crystal structure the Fab fragment of Efalizumab in complex with LFA-1 I domain, Form I

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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