1p53

From Proteopedia

(Difference between revisions)

Current revision

The Crystal Structure of ICAM-1 D3-D5 fragment

Structural highlights

1p53 is a 2 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 3.06Å
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

We have determined the 3.0 A crystal structure of the three C-terminal domains 3-5 (D3-D5) of ICAM-1. Combined with the previously known N-terminal two-domain structure (D1D2), a model of an entire ICAM-1 extracellular fragment has been constructed. This model should represent a general architecture of other ICAM family members, particularly ICAM-3 and ICAM-5. The observed intimate dimerization interaction at D4 and a stiff D4-D5 stem-like architecture provide a good structural explanation for the existence of preformed ICAM-1 cis dimers on the cell membrane. Together with another dimerization interface at D1, a band-like one-dimensional linear cluster of ICAM-1 on an antigen-presenting cell (APC) surface can be envisioned, which might explain the formation of an immunological synapse between an activated T cell and APC which is critical for T cell receptor signaling.

Structural basis for dimerization of ICAM-1 on the cell surface.,Yang Y, Jun CD, Liu JH, Zhang R, Joachimiak A, Springer TA, Wang JH Mol Cell. 2004 Apr 23;14(2):269-76. PMID:15099525^[5]

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

References

↑ 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
↑ 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
↑ 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
↑ 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
↑ Yang Y, Jun CD, Liu JH, Zhang R, Joachimiak A, Springer TA, Wang JH. Structural basis for dimerization of ICAM-1 on the cell surface. Mol Cell. 2004 Apr 23;14(2):269-76. PMID:15099525

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/1p53"

@@ Line 1: / Line 1: @@
 ==The Crystal Structure of ICAM-1 D3-D5 fragment==
-<StructureSection load='1p53' size='340' side='right' caption='[[1p53]], [[Resolution|resolution]] 3.06&Aring;' scene=''>
+<StructureSection load='1p53' size='340' side='right'caption='[[1p53]], [[Resolution|resolution]] 3.06&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1p53]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P53 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P53 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1p53]] is a 2 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=1P53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P53 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene><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]] 3.06&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ICAM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p53 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p53 RCSB], [http://www.ebi.ac.uk/pdbsum/1p53 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=1p53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p53 OCA], [https://pdbe.org/1p53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p53 RCSB], [https://www.ebi.ac.uk/pdbsum/1p53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p53 ProSAT]</span></td></tr>
-<table>
+</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/p5/1p53_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p5/1p53_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1p53 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 25: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1p53" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 33: / Line 37: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Jochimiak, A.]]
+[[Category: Large Structures]]
-[[Category: Jun, C D.]]
+[[Category: Jochimiak A]]
-[[Category: Liu, J H.]]
+[[Category: Jun CD]]
-[[Category: Springer, T A.]]
+[[Category: Liu JH]]
-[[Category: Wang, J H.]]
+[[Category: Springer TA]]
-[[Category: Yang, Y.]]
+[[Category: Wang JH]]
-[[Category: Zhang, R.]]
+[[Category: Yang Y]]
-[[Category: Beta-sheet]]
+[[Category: Zhang R]]
-[[Category: Cell adhesion]]
-[[Category: Dimer]]
-[[Category: Igsf domain]]

1p53

From Proteopedia

Current revision

The Crystal Structure of ICAM-1 D3-D5 fragment

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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