1hng: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(14 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1hng.jpg|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1hng", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_1hng|  PDB=1hng  |  SCENE=  }}
'''CRYSTAL STRUCTURE AT 2.8 ANGSTROMS RESOLUTION OF A SOLUBLE FORM OF THE CELL ADHESION MOLECULE CD2'''


==CRYSTAL STRUCTURE AT 2.8 ANGSTROMS RESOLUTION OF A SOLUBLE FORM OF THE CELL ADHESION MOLECULE CD2==
<StructureSection load='1hng' size='340' side='right'caption='[[1hng]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hng]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HNG 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]] 2.8&#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=1hng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hng OCA], [https://pdbe.org/1hng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hng RCSB], [https://www.ebi.ac.uk/pdbsum/1hng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hng ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CD2_RAT CD2_RAT] CD2 interacts with lymphocyte function-associated antigen (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T-cells, the cytoplasmic domain is implicated in the signaling function.
== 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/hn/1hng_consurf.spt"</scriptWhenChecked>
    <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/main_output.php?pdb_ID=1hng ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of a soluble form of the T lymphocyte antigen CD2 provides the first complete view of the extracellular region of a cell adhesion molecule. The topology of the molecule, which comprises two immunoglobulin-like domains, is the same as that of the first two domains of CD4 but the relative domain orientation is altered by a fairly flexible linker region. The putative ligand-binding beta-sheet forms a flat surface towards the top of the molecule. Crystal contacts between these surfaces suggest a plausible model for the adhesive interaction.


==Overview==
Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2.,Jones EY, Davis SJ, Williams AF, Harlos K, Stuart DI Nature. 1992 Nov 19;360(6401):232-9. PMID:1279440<ref>PMID:1279440</ref>
The crystal structure of a soluble form of the T lymphocyte antigen CD2 provides the first complete view of the extracellular region of a cell adhesion molecule. The topology of the molecule, which comprises two immunoglobulin-like domains, is the same as that of the first two domains of CD4 but the relative domain orientation is altered by a fairly flexible linker region. The putative ligand-binding beta-sheet forms a flat surface towards the top of the molecule. Crystal contacts between these surfaces suggest a plausible model for the adhesive interaction.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1HNG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HNG OCA].
</div>
<div class="pdbe-citations 1hng" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2., Jones EY, Davis SJ, Williams AF, Harlos K, Stuart DI, Nature. 1992 Nov 19;360(6401):232-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1279440 1279440]
*[[CD2|CD2]]
[[Category: Rattus norvegicus]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Davis, S J.]]
__TOC__
[[Category: Harlos, K.]]
</StructureSection>
[[Category: Jones, E Y.]]
[[Category: Large Structures]]
[[Category: Stuart, D I.]]
[[Category: Rattus rattus]]
[[Category: Williams, A F.]]
[[Category: Davis SJ]]
[[Category: T lymphocyte adhesion glycoprotein]]
[[Category: Harlos K]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:02:25 2008''
[[Category: Jones EY]]
[[Category: Stuart DI]]
[[Category: Williams AF]]

Latest revision as of 09:42, 30 October 2024

CRYSTAL STRUCTURE AT 2.8 ANGSTROMS RESOLUTION OF A SOLUBLE FORM OF THE CELL ADHESION MOLECULE CD2CRYSTAL STRUCTURE AT 2.8 ANGSTROMS RESOLUTION OF A SOLUBLE FORM OF THE CELL ADHESION MOLECULE CD2

Structural highlights

1hng is a 2 chain structure with sequence from Rattus rattus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CD2_RAT CD2 interacts with lymphocyte function-associated antigen (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T-cells, the cytoplasmic domain is implicated in the signaling function.

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

The crystal structure of a soluble form of the T lymphocyte antigen CD2 provides the first complete view of the extracellular region of a cell adhesion molecule. The topology of the molecule, which comprises two immunoglobulin-like domains, is the same as that of the first two domains of CD4 but the relative domain orientation is altered by a fairly flexible linker region. The putative ligand-binding beta-sheet forms a flat surface towards the top of the molecule. Crystal contacts between these surfaces suggest a plausible model for the adhesive interaction.

Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2.,Jones EY, Davis SJ, Williams AF, Harlos K, Stuart DI Nature. 1992 Nov 19;360(6401):232-9. PMID:1279440[1]

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

See Also

References

  1. ↑ Jones EY, Davis SJ, Williams AF, Harlos K, Stuart DI. Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2. Nature. 1992 Nov 19;360(6401):232-9. PMID:1279440 doi:http://dx.doi.org/10.1038/360232a0

1hng, resolution 2.80Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1hng&oldid=4198706"