1zon: Difference between revisions

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New page: left|200px<br /> <applet load="1zon" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zon, resolution 2.0Å" /> '''CD11A I-DOMAIN WITHO...
 
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[[Image:1zon.gif|left|200px]]<br />
<applet load="1zon" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1zon, resolution 2.0&Aring;" />
'''CD11A I-DOMAIN WITHOUT BOUND CATION'''<br />


==Overview==
==CD11A I-DOMAIN WITHOUT BOUND CATION==
BACKGROUND: The integrin family of cell-surface receptors mediates a wide, variety of cell-cell and cell-extracellular matrix interactions., Integrin-ligand interactions are invariably dependent on the presence of, divalent cations, and a subset of integrins contain a approximately 200, amino acid inserted (I) domain that is important for ligand binding, activity and contains a single divalent cation binding site. Many, integrins are believed to respond to stimuli by undergoing a, conformational change that increases their affinity for ligand, and there, is a clear difference between two crystal structures of the CD11b I domain, with different divalent cations (magnesium and manganese) bound. In, addition to the different bound cation, a 'ligand mimetic' crystal lattice, interaction in the CD11b I domain structure with bound magnesium has led, to the interpretation that the different CD11b I domain structures, represent different affinity states of I domains. The influence of the, bound cation on I domain structure and function remains incompletely, understood, however. The crystal structure of the CD11a I domain bound to, manganese is known. We therefore set out to determine whether this, structure changes when the metal ion is altered or removed. RESULTS: We, report here the crystal structures of the CD11a I domain determined in the, absence of bound metal ion and with bound magnesium ion. No major, structural rearrangements are observed in the metal-binding site of the, CD11a I domain in the absence or presence of bound manganese ion. The, structures of the CD11a I domain with magnesium or manganese bound are, extremely similar. CONCLUSIONS: The conformation of the CD11a I domain is, not altered by changes in metal ion binding. The cation-dependence of, ligand binding thus indicates that the metal ion is either involved in, direct interaction with ligand or required to promote a favorable, quaternary arrangement of the integrin.
<StructureSection load='1zon' size='340' side='right'caption='[[1zon]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1zon]] is a 1 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=1ZON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZON 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&#8491;</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=1zon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zon OCA], [https://pdbe.org/1zon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zon RCSB], [https://www.ebi.ac.uk/pdbsum/1zon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zon 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/zo/1zon_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=1zon ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1ZON is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZON OCA].
*[[Integrin 3D structures|Integrin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The role of the divalent cation in the structure of the I domain from the CD11a/CD18 integrin., Qu A, Leahy DJ, Structure. 1996 Aug 15;4(8):931-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8805579 8805579]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Leahy, D.J.]]
[[Category: Leahy DJ]]
[[Category: Qu, A.]]
[[Category: Qu A]]
[[Category: cell adhesion]]
[[Category: cytoskeleton]]
[[Category: extracellular matrix]]
[[Category: glycoprotein]]
[[Category: integrin]]
[[Category: signal]]
[[Category: transmembrane]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:37:53 2007''

Latest revision as of 12:06, 14 February 2024

CD11A I-DOMAIN WITHOUT BOUND CATIONCD11A I-DOMAIN WITHOUT BOUND CATION

Structural highlights

1zon 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.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1zon, resolution 2.00Å

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