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1t0p

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Structural Basis of ICAM recognition by integrin alpahLbeta2 revealed in the complex structure of binding domains of ICAM-3 and alphaLbeta2 at 1.65 A

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Retrieved from "http://52.214.119.220/wiki/index.php/1t0p"

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-[[Image:1t0p.gif|left|200px]]<br />
-<applet load="1t0p" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1t0p, resolution 1.66&Aring;" />
-'''Structural Basis of ICAM recognition by integrin alpahLbeta2 revealed in the complex structure of binding domains of ICAM-3 and alphaLbeta2 at 1.65 A'''<br />
-==Overview==
+==Structural Basis of ICAM recognition by integrin alpahLbeta2 revealed in the complex structure of binding domains of ICAM-3 and alphaLbeta2 at 1.65 A==
-Within the Ig superfamily (IgSF), intercellular adhesion molecules (ICAMs), form a subfamily that binds the leukocyte integrin alphaLbeta2. We report, a 1.65-A-resolution crystal structure of the ICAM-3 N-terminal domain (D1), in complex with the inserted domain, the ligand-binding domain of, alphaLbeta2. This high-resolution structure and comparisons among ICAM, subfamily members establish that the binding of ICAM-3 D1 onto the, inserted domain represents a common docking mode for ICAM subfamily, members. The markedly different off-rates of ICAM-1, -2, and -3 appear to, be determined by the hydrophobicity of residues that surround a metal, coordination bond in the alphaLbeta2-binding interfaces. Variation in, composition of glycans on the periphery of the interfaces influences, on-rate.
+<StructureSection load='1t0p' size='340' side='right'caption='[[1t0p]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1t0p]] 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=1T0P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T0P 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]] 1.66&#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=1t0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0p OCA], [https://pdbe.org/1t0p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t0p RCSB], [https://www.ebi.ac.uk/pdbsum/1t0p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t0p ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ITAL_HUMAN ITAL_HUMAN] Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. It is involved in a variety of immune phenomena including leukocyte-endothelial cell interaction, cytotoxic T-cell mediated killing, and antibody dependent killing by granulocytes and monocytes.
+== 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/t0/1t0p_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=1t0p ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-T0P 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=1T0P OCA].
+*[[Integrin 3D structures|Integrin 3D structures]]
+*[[Intercellular adhesion molecule|Intercellular adhesion molecule]]
-==Reference==
+__TOC__
-An atomic resolution view of ICAM recognition in a complex between the binding domains of ICAM-3 and integrin alphaLbeta2., Song G, Yang Y, Liu JH, Casasnovas JM, Shimaoka M, Springer TA, Wang JH, Proc Natl Acad Sci U S A. 2005 Mar 1;102(9):3366-71. Epub 2005 Feb 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15728350 15728350]
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Liu, J.H.]]
+[[Category: Liu JH]]
-[[Category: Shimaoko, M.]]
+[[Category: Shimaoko M]]
-[[Category: Song, G.]]
+[[Category: Song G]]
-[[Category: Springer, T.A.]]
+[[Category: Springer TA]]
-[[Category: Wang, J.H.]]
+[[Category: Wang JH]]
-[[Category: Yang, Y.T.]]
+[[Category: Yang YT]]
-[[Category: MG]]
-[[Category: NAG]]
-[[Category: rossmann fold; ig-super family domain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:18:52 2007''

1t0p

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Structural Basis of ICAM recognition by integrin alpahLbeta2 revealed in the complex structure of binding domains of ICAM-3 and alphaLbeta2 at 1.65 A

Structural highlights

Function

Evolutionary Conservation

See Also

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