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New page: left|200px<br /> <applet load="2oz4" size="450" color="white" frame="true" align="right" spinBox="true" caption="2oz4, resolution 2.70Å" /> '''Structural Plastici...
 
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[[Image:2oz4.gif|left|200px]]<br />
<applet load="2oz4" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2oz4, resolution 2.70&Aring;" />
'''Structural Plasticity in IgSF Domain 4 of ICAM-1 Mediates Cell Surface Dimerization'''<br />


==Overview==
==Structural Plasticity in IgSF Domain 4 of ICAM-1 Mediates Cell Surface Dimerization==
The Ig superfamily (IgSF) intercellular adhesion molecule-1 (ICAM-1), equilibrates between monomeric and dimeric forms on the cell surface, and, dimerization enhances cell adhesion. A crystal structure of ICAM-1 IgSF, domains (D) 3-5 revealed a unique dimerization interface in which D4s of, two protomers fuse through edge beta-strands to form a single super, beta-sandwich domain. Here, we describe a crystal structure at 2.7-A, resolution of monomeric ICAM-1 D3-D5, stabilized by the monomer-specific, Fab CA7. CA7 binds to D5 in a region that is buried in the dimeric, interface and is distal from the dimerization site in D4. In monomeric, ICAM-1 D3-D5, a 16-residue loop in D4 that is disordered in the dimeric, structure could clearly be traced as a BC loop, a short C strand, and a CE, meander with a cis-Pro followed by a solvent-exposed, flexible, four-residue region. Deletions of 6 or 10 residues showed that the, C-strand is essential for monomer stability, whereas a distinct, six-residue deletion showed little contribution of the CE meander., Mutation of two inward-pointing Leu residues in edge beta-strand E to Lys, increased monomer stability, confirming the hypothesis that, inward-pointing charged side chains on edge beta-strands are an important, design feature to prevent beta-supersheet formation. Overall, the studies, reveal that monomer-dimer transition is associated with a surprisingly, large, physiologically relevant, IgSF domain rearrangement.
<StructureSection load='2oz4' size='340' side='right'caption='[[2oz4]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2oz4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OZ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OZ4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2oz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oz4 OCA], [https://pdbe.org/2oz4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oz4 RCSB], [https://www.ebi.ac.uk/pdbsum/2oz4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oz4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ICAM1_HUMAN ICAM1_HUMAN] ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation. In case of rhinovirus infection acts as a cellular receptor for the virus.<ref>PMID:2538243</ref> <ref>PMID:1968231</ref> <ref>PMID:11173916</ref> <ref>PMID:17875742</ref>
== 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/oz/2oz4_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/main_output.php?pdb_ID=2oz4 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Ig superfamily (IgSF) intercellular adhesion molecule-1 (ICAM-1) equilibrates between monomeric and dimeric forms on the cell surface, and dimerization enhances cell adhesion. A crystal structure of ICAM-1 IgSF domains (D) 3-5 revealed a unique dimerization interface in which D4s of two protomers fuse through edge beta-strands to form a single super beta-sandwich domain. Here, we describe a crystal structure at 2.7-A resolution of monomeric ICAM-1 D3-D5, stabilized by the monomer-specific Fab CA7. CA7 binds to D5 in a region that is buried in the dimeric interface and is distal from the dimerization site in D4. In monomeric ICAM-1 D3-D5, a 16-residue loop in D4 that is disordered in the dimeric structure could clearly be traced as a BC loop, a short C strand, and a CE meander with a cis-Pro followed by a solvent-exposed, flexible four-residue region. Deletions of 6 or 10 residues showed that the C-strand is essential for monomer stability, whereas a distinct six-residue deletion showed little contribution of the CE meander. Mutation of two inward-pointing Leu residues in edge beta-strand E to Lys increased monomer stability, confirming the hypothesis that inward-pointing charged side chains on edge beta-strands are an important design feature to prevent beta-supersheet formation. Overall, the studies reveal that monomer-dimer transition is associated with a surprisingly large, physiologically relevant, IgSF domain rearrangement.


==Disease==
Structural plasticity in Ig superfamily domain 4 of ICAM-1 mediates cell surface dimerization.,Chen X, Kim TD, Carman CV, Mi LZ, Song G, Springer TA Proc Natl Acad Sci U S A. 2007 Sep 25;104(39):15358-63. Epub 2007 Sep 19. PMID:17881562<ref>PMID:17881562</ref>
Known disease associated with this structure: Malaria, cerebral, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147840 147840]]


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2OZ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG, SO4, ZN and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OZ4 OCA].
</div>
<div class="pdbe-citations 2oz4" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structural plasticity in Ig superfamily domain 4 of ICAM-1 mediates cell surface dimerization., Chen X, Kim TD, Carman CV, Mi LZ, Song G, Springer TA, Proc Natl Acad Sci U S A. 2007 Sep 25;104(39):15358-63. Epub 2007 Sep 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17881562 17881562]
*[[Antibody 3D structures|Antibody 3D structures]]
*[[Intercellular adhesion molecule|Intercellular adhesion molecule]]
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Carman CV]]
[[Category: Carman, C.V.]]
[[Category: Chen X]]
[[Category: Chen, X.]]
[[Category: Kim TD]]
[[Category: Kim, T.D.]]
[[Category: Mi L]]
[[Category: Mi, L.]]
[[Category: Song G]]
[[Category: Song, G.]]
[[Category: Springer TA]]
[[Category: Springer, T.A.]]
[[Category: NAG]]
[[Category: SO4]]
[[Category: TRS]]
[[Category: ZN]]
[[Category: cell adhesion]]
[[Category: cell-surface dimerization]]
[[Category: igsf domain]]
[[Category: structural plasticity]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:18:23 2007''

Latest revision as of 13:51, 30 August 2023

Structural Plasticity in IgSF Domain 4 of ICAM-1 Mediates Cell Surface DimerizationStructural Plasticity in IgSF Domain 4 of ICAM-1 Mediates Cell Surface Dimerization

Structural highlights

2oz4 is a 3 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ICAM1_HUMAN ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation. In case of rhinovirus infection acts as a cellular receptor for the virus.[1] [2] [3] [4]

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

The Ig superfamily (IgSF) intercellular adhesion molecule-1 (ICAM-1) equilibrates between monomeric and dimeric forms on the cell surface, and dimerization enhances cell adhesion. A crystal structure of ICAM-1 IgSF domains (D) 3-5 revealed a unique dimerization interface in which D4s of two protomers fuse through edge beta-strands to form a single super beta-sandwich domain. Here, we describe a crystal structure at 2.7-A resolution of monomeric ICAM-1 D3-D5, stabilized by the monomer-specific Fab CA7. CA7 binds to D5 in a region that is buried in the dimeric interface and is distal from the dimerization site in D4. In monomeric ICAM-1 D3-D5, a 16-residue loop in D4 that is disordered in the dimeric structure could clearly be traced as a BC loop, a short C strand, and a CE meander with a cis-Pro followed by a solvent-exposed, flexible four-residue region. Deletions of 6 or 10 residues showed that the C-strand is essential for monomer stability, whereas a distinct six-residue deletion showed little contribution of the CE meander. Mutation of two inward-pointing Leu residues in edge beta-strand E to Lys increased monomer stability, confirming the hypothesis that inward-pointing charged side chains on edge beta-strands are an important design feature to prevent beta-supersheet formation. Overall, the studies reveal that monomer-dimer transition is associated with a surprisingly large, physiologically relevant, IgSF domain rearrangement.

Structural plasticity in Ig superfamily domain 4 of ICAM-1 mediates cell surface dimerization.,Chen X, Kim TD, Carman CV, Mi LZ, Song G, Springer TA Proc Natl Acad Sci U S A. 2007 Sep 25;104(39):15358-63. Epub 2007 Sep 19. PMID:17881562[5]

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

See Also

References

  1. ↑ Greve JM, Davis G, Meyer AM, Forte CP, Yost SC, Marlor CW, Kamarck ME, McClelland A. The major human rhinovirus receptor is ICAM-1. Cell. 1989 Mar 10;56(5):839-47. PMID:2538243
  2. ↑ Marlin SD, Staunton DE, Springer TA, Stratowa C, Sommergruber W, Merluzzi VJ. A soluble form of intercellular adhesion molecule-1 inhibits rhinovirus infection. Nature. 1990 Mar 1;344(6261):70-2. PMID:1968231 doi:http://dx.doi.org/10.1038/344070a0
  3. ↑ Hayashi T, Takahashi T, Motoya S, Ishida T, Itoh F, Adachi M, Hinoda Y, Imai K. MUC1 mucin core protein binds to the domain 1 of ICAM-1. Digestion. 2001;63 Suppl 1:87-92. PMID:11173916
  4. ↑ van Buul JD, Allingham MJ, Samson T, Meller J, Boulter E, Garcia-Mata R, Burridge K. RhoG regulates endothelial apical cup assembly downstream from ICAM1 engagement and is involved in leukocyte trans-endothelial migration. J Cell Biol. 2007 Sep 24;178(7):1279-93. Epub 2007 Sep 17. PMID:17875742 doi:10.1083/jcb.200612053
  5. ↑ Chen X, Kim TD, Carman CV, Mi LZ, Song G, Springer TA. Structural plasticity in Ig superfamily domain 4 of ICAM-1 mediates cell surface dimerization. Proc Natl Acad Sci U S A. 2007 Sep 25;104(39):15358-63. Epub 2007 Sep 19. PMID:17881562

2oz4, resolution 2.70Å

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