2pet: Difference between revisions

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{{Seed}}
[[Image:2pet.png|left|200px]]


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==Lutheran glycoprotein, N-terminal domains 1 and 2.==
The line below this paragraph, containing "STRUCTURE_2pet", creates the "Structure Box" on the page.
<StructureSection load='2pet' size='340' side='right'caption='[[2pet]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2pet]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PET FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BCAM, LU, MSK19 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pet OCA], [https://pdbe.org/2pet PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pet RCSB], [https://www.ebi.ac.uk/pdbsum/2pet PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pet ProSAT]</span></td></tr>
{{STRUCTURE_2pet|  PDB=2pet  |  SCENE=  }}
</table>
== Function ==
[[https://www.uniprot.org/uniprot/BCAM_HUMAN BCAM_HUMAN]] Laminin alpha-5 receptor. May mediate intracellular signaling.<ref>PMID:9616226</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/pe/2pet_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=2pet ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Lutheran blood group glycoprotein, first discovered on erythrocytes, is widely expressed in human tissues. It is a ligand for the alpha5 subunit of Laminin 511/521, an extracellular matrix protein. This interaction may contribute to vaso-occlusive events that are an important cause of morbidity in sickle cell disease. Using x-ray crystallography, small-angle x-ray scattering, and site-directed mutagenesis, we show that the extracellular region of Lutheran forms an extended structure with a distinctive bend between the second and third immunoglobulin-like domains. The linker between domains 2 and 3 appears to be flexible and is a critical determinant in maintaining an overall conformation for Lutheran that is capable of binding to Laminin. Mutagenesis studies indicate that Asp312 of Lutheran and the surrounding cluster of negatively charged residues in this linker region form the Laminin-binding site. Unusually, receptor binding is therefore not a function of the domains expected to be furthermost from the plasma membrane. These studies imply that structural flexibility of Lutheran may be essential for its interaction with Laminin and present a novel opportunity for the development of therapeutics for sickle cell disease.


===Lutheran glycoprotein, N-terminal domains 1 and 2.===
The Laminin 511/521-binding site on the Lutheran blood group glycoprotein is located at the flexible junction of Ig domains 2 and 3.,Mankelow TJ, Burton N, Stefansdottir FO, Spring FA, Parsons SF, Pedersen JS, Oliveira CL, Lammie D, Wess T, Mohandas N, Chasis JA, Brady RL, Anstee DJ Blood. 2007 Nov 1;110(9):3398-406. Epub 2007 Jul 17. PMID:17638854<ref>PMID:17638854</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
The line below this paragraph, {{ABSTRACT_PUBMED_17638854}}, adds the Publication Abstract to the page
<div class="pdbe-citations 2pet" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 17638854 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_17638854}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Human]]
2PET is a 1 chain structure of 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=2PET OCA].
[[Category: Large Structures]]
 
[[Category: Brady, R L]]
==Reference==
[[Category: Burton, N]]
<ref group="xtra">PMID:17638854</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Brady, R L.]]
[[Category: Burton, N.]]
[[Category: Cell adhesion]]
[[Category: Cell adhesion]]
[[Category: Immunoglobulin superfamily.]]
[[Category: Immunoglobulin superfamily]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 11:07:38 2009''

Latest revision as of 18:22, 17 June 2021

Lutheran glycoprotein, N-terminal domains 1 and 2.Lutheran glycoprotein, N-terminal domains 1 and 2.

Structural highlights

2pet is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:BCAM, LU, MSK19 (HUMAN)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BCAM_HUMAN] Laminin alpha-5 receptor. May mediate intracellular signaling.[1]

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 Lutheran blood group glycoprotein, first discovered on erythrocytes, is widely expressed in human tissues. It is a ligand for the alpha5 subunit of Laminin 511/521, an extracellular matrix protein. This interaction may contribute to vaso-occlusive events that are an important cause of morbidity in sickle cell disease. Using x-ray crystallography, small-angle x-ray scattering, and site-directed mutagenesis, we show that the extracellular region of Lutheran forms an extended structure with a distinctive bend between the second and third immunoglobulin-like domains. The linker between domains 2 and 3 appears to be flexible and is a critical determinant in maintaining an overall conformation for Lutheran that is capable of binding to Laminin. Mutagenesis studies indicate that Asp312 of Lutheran and the surrounding cluster of negatively charged residues in this linker region form the Laminin-binding site. Unusually, receptor binding is therefore not a function of the domains expected to be furthermost from the plasma membrane. These studies imply that structural flexibility of Lutheran may be essential for its interaction with Laminin and present a novel opportunity for the development of therapeutics for sickle cell disease.

The Laminin 511/521-binding site on the Lutheran blood group glycoprotein is located at the flexible junction of Ig domains 2 and 3.,Mankelow TJ, Burton N, Stefansdottir FO, Spring FA, Parsons SF, Pedersen JS, Oliveira CL, Lammie D, Wess T, Mohandas N, Chasis JA, Brady RL, Anstee DJ Blood. 2007 Nov 1;110(9):3398-406. Epub 2007 Jul 17. PMID:17638854[2]

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

References

  1. ↑ Udani M, Zen Q, Cottman M, Leonard N, Jefferson S, Daymont C, Truskey G, Telen MJ. Basal cell adhesion molecule/lutheran protein. The receptor critical for sickle cell adhesion to laminin. J Clin Invest. 1998 Jun 1;101(11):2550-8. PMID:9616226 doi:http://dx.doi.org/10.1172/JCI1204
  2. ↑ Mankelow TJ, Burton N, Stefansdottir FO, Spring FA, Parsons SF, Pedersen JS, Oliveira CL, Lammie D, Wess T, Mohandas N, Chasis JA, Brady RL, Anstee DJ. The Laminin 511/521-binding site on the Lutheran blood group glycoprotein is located at the flexible junction of Ig domains 2 and 3. Blood. 2007 Nov 1;110(9):3398-406. Epub 2007 Jul 17. PMID:17638854 doi:10.1182/blood-2007-06-094748

2pet, resolution 1.70Å

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