1d3l

From Proteopedia

(Difference between revisions)

Revision as of 04:11, 30 August 2017

D1D2-ICAM-1 FULLY GLYCOSYLATED, VARIATION OF D1-D2 INTERDOMAIN ANGLE IN DIFFERENT CRYSTAL STRUCTURES.

Structural highlights

1d3l is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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

Two human rhinovirus serotypes complexed with two- and five-domain soluble fragments of the cellular receptor, intercellular adhesion molecule-1, have been investigated by X-ray crystallographic analyses of the individual components and by cryo-electron microscopy of the complexes. The three-dimensional image reconstructions provide a molecular envelope within which the crystal structures of the viruses and the receptor fragments can be positioned with accuracy. The N-terminal domain of the receptor binds to the rhinovirus 'canyon' surrounding the icosahedral 5-fold axes. Fitting of molecular models into the image reconstruction density identified the residues on the virus that interact with those on the receptor surface, demonstrating complementarity of the electrostatic patterns for the tip of the N-terminal receptor domain and the floor of the canyon. The complexes seen in the image reconstructions probably represent the first stage of a multistep binding process. A mechanism is proposed for the subsequent viral uncoating process.

Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor.,Kolatkar PR, Bella J, Olson NH, Bator CM, Baker TS, Rossmann MG EMBO J. 1999 Nov 15;18(22):6249-59. PMID:10562537^[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
↑ Kolatkar PR, Bella J, Olson NH, Bator CM, Baker TS, Rossmann MG. Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor. EMBO J. 1999 Nov 15;18(22):6249-59. PMID:10562537 doi:10.1093/emboj/18.22.6249

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/1d3l"

@@ Line 1: / Line 1: @@
 ==D1D2-ICAM-1 FULLY GLYCOSYLATED, VARIATION OF D1-D2 INTERDOMAIN ANGLE IN DIFFERENT CRYSTAL STRUCTURES.==
 <StructureSection load='1d3l' size='340' side='right' caption='[[1d3l]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1d3l]] is a 1 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=1D3L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1D3L FirstGlance]. <br>
-</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=1d3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d3l OCA], [http://pdbe.org/1d3l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1d3l RCSB], [http://www.ebi.ac.uk/pdbsum/1d3l PDBsum]</span></td></tr>
+</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=1d3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d3l OCA], [http://pdbe.org/1d3l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1d3l RCSB], [http://www.ebi.ac.uk/pdbsum/1d3l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1d3l ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
     <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=1d3l ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1d3l

From Proteopedia

Revision as of 04:11, 30 August 2017

D1D2-ICAM-1 FULLY GLYCOSYLATED, VARIATION OF D1-D2 INTERDOMAIN ANGLE IN DIFFERENT CRYSTAL STRUCTURES.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox