1mq8: Difference between revisions

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New page: left|200px<br /> <applet load="1mq8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mq8, resolution 3.30Å" /> '''Crystal structure o...
 
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[[Image:1mq8.gif|left|200px]]<br />
<applet load="1mq8" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1mq8, resolution 3.30&Aring;" />
'''Crystal structure of alphaL I domain in complex with ICAM-1'''<br />


==Overview==
==Crystal structure of alphaL I domain in complex with ICAM-1==
The structure of the I domain of integrin alpha L beta 2 bound to the Ig, superfamily ligand ICAM-1 reveals the open ligand binding conformation and, the first example of an integrin-IgSF interface. The I domain Mg2+, directly coordinates Glu-34 of ICAM-1, and a dramatic swing of I domain, residue Glu-241 enables a critical salt bridge. Liganded and unliganded, structures for both high- and intermediate-affinity mutant I domains, reveal that ligand binding can induce conformational change in the alpha L, I domain and that allosteric signals can convert the closed conformation, to intermediate or open conformations without ligand binding. Pulling down, on the C-terminal alpha 7 helix with introduced disulfide bonds ratchets, the beta 6-alpha 7 loop into three different positions in the closed, intermediate, and open conformations, with a progressive increase in, affinity.
<StructureSection load='1mq8' size='340' side='right'caption='[[1mq8]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mq8]] is a 4 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=1MQ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MQ8 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]] 3.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1mq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mq8 OCA], [https://pdbe.org/1mq8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mq8 RCSB], [https://www.ebi.ac.uk/pdbsum/1mq8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mq8 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/mq/1mq8_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=1mq8 ConSurf].
<div style="clear:both"></div>


==Disease==
==See Also==
Known disease associated with this structure: Malaria, cerebral, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147840 147840]]
*[[Integrin 3D structures|Integrin 3D structures]]
 
*[[Intercellular adhesion molecule|Intercellular adhesion molecule]]
==About this Structure==
== References ==
1MQ8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MQ8 OCA].
<references/>
 
__TOC__
==Reference==
</StructureSection>
Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation., Shimaoka M, Xiao T, Liu JH, Yang Y, Dong Y, Jun CD, McCormack A, Zhang R, Joachimiak A, Takagi J, Wang JH, Springer TA, Cell. 2003 Jan 10;112(1):99-111. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12526797 12526797]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Dong, Y.]]
[[Category: Dong Y]]
[[Category: Joachimiak, A.]]
[[Category: Joachimiak A]]
[[Category: Jun, C.D.]]
[[Category: Jun C-D]]
[[Category: Liu, J.H.]]
[[Category: Liu J-H]]
[[Category: McCormack, A.]]
[[Category: McCormack A]]
[[Category: Shimaoka, M.]]
[[Category: Shimaoka M]]
[[Category: Springer, T.A.]]
[[Category: Springer TA]]
[[Category: Takagi, J.]]
[[Category: Takagi J]]
[[Category: Wang, J.H.]]
[[Category: Wang J-H]]
[[Category: Xiao, T.]]
[[Category: Xiao T]]
[[Category: Yang, Y.]]
[[Category: Yang Y]]
[[Category: Zhang, R.]]
[[Category: Zhang R]]
[[Category: MG]]
[[Category: NAG]]
[[Category: ig superfamily]]
[[Category: metal mediated protein interface]]
[[Category: rossmann fold]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:14:03 2007''

Latest revision as of 11:39, 10 April 2024

Crystal structure of alphaL I domain in complex with ICAM-1Crystal structure of alphaL I domain in complex with ICAM-1

Structural highlights

1mq8 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.3Å
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.

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

1mq8, resolution 3.30Å

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