1j19

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the radxin FERM domain complexed with the ICAM-2 cytoplasmic peptide

Structural highlights

1j19 is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RADI_MOUSE Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane.

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

ERM (ezrin/radixin/moesin) proteins recognize the cytoplasmic domains of adhesion molecules in the formation of the membrane-associated cytoskeleton. Here we report the crystal structure of the radixin FERM (4.1 and ERM) domain complexed with the ICAM-2 cytoplasmic peptide. The non-polar region of the ICAM-2 peptide contains the RxxTYxVxxA sequence motif to form a beta-strand followed by a short 3(10)-helix. It binds the groove of the phosphotyrosine-binding (PTB)-like subdomain C mediated by a beta-beta association and several side-chain interactions. The binding mode of the ICAM-2 peptide to the FERM domain is distinct from that of the NPxY motif-containing peptide binding to the canonical PTB domain. Mutation analyses based on the crystal structure reveal the determinant elements of recognition and provide the first insights into the physical link between adhesion molecules and ERM proteins.

Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex.,Hamada K, Shimizu T, Yonemura S, Tsukita S, Tsukita S, Hakoshima T EMBO J. 2003 Feb 3;22(3):502-14. PMID:12554651^[1]

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

References

↑ Hamada K, Shimizu T, Yonemura S, Tsukita S, Tsukita S, Hakoshima T. Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex. EMBO J. 2003 Feb 3;22(3):502-14. PMID:12554651 doi:10.1093/emboj/cdg039

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/1j19"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the radxin FERM domain complexed with the ICAM-2 cytoplasmic peptide==
-<StructureSection load='1j19' size='340' side='right' caption='[[1j19]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='1j19' size='340' side='right'caption='[[1j19]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1j19]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J19 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J19 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1j19]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J19 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gc6|1gc6]], [[1gc7|1gc7]], [[1ef1|1ef1]], [[1e5w|1e5w]], [[1isn|1isn]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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=1j19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j19 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1j19 RCSB], [http://www.ebi.ac.uk/pdbsum/1j19 PDBsum]</span></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=1j19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j19 OCA], [https://pdbe.org/1j19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j19 RCSB], [https://www.ebi.ac.uk/pdbsum/1j19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j19 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RADI_MOUSE RADI_MOUSE]] Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane. [[http://www.uniprot.org/uniprot/ICAM2_MOUSE ICAM2_MOUSE]] ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). ICAM2 may play a role in lymphocyte recirculation by blocking LFA-1-dependent cell adhesion. It mediates adhesive interactions important for antigen-specific immune response, NK-cell mediated clearance, lymphocyte recirculation, and other cellular interactions important for immune response and surveillance.
+[https://www.uniprot.org/uniprot/RADI_MOUSE RADI_MOUSE] Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j1/1j19_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j1/1j19_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1j19 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 26: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1j19" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Radixin|Radixin]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Hakoshima, T]]
+[[Category: Hakoshima T]]
-[[Category: Hamada, K]]
+[[Category: Hamada K]]
-[[Category: Shimizu, T]]
+[[Category: Shimizu T]]
-[[Category: Tsukita, S]]
+[[Category: Tsukita S]]
-[[Category: Yonemura, S]]
+[[Category: Yonemura S]]
-[[Category: Cell adhesion]]
-[[Category: Protein-peptide complex]]

1j19

From Proteopedia

Current revision

Crystal structure of the radxin FERM domain complexed with the ICAM-2 cytoplasmic peptide

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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