1by2: Difference between revisions

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==STRUCTURE OF M2BP SCAVENGER RECEPTOR CYSTEINE-RICH DOMAIN==
==STRUCTURE OF M2BP SCAVENGER RECEPTOR CYSTEINE-RICH DOMAIN==
<StructureSection load='1by2' size='340' side='right' caption='[[1by2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1by2' size='340' side='right'caption='[[1by2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1by2]] 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=1BY2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BY2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1by2]] 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=1BY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BY2 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1by2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1by2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1by2 RCSB], [http://www.ebi.ac.uk/pdbsum/1by2 PDBsum]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<table>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1by2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1by2 OCA], [https://pdbe.org/1by2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1by2 RCSB], [https://www.ebi.ac.uk/pdbsum/1by2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1by2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LG3BP_HUMAN LG3BP_HUMAN] Promotes intergrin-mediated cell adhesion. May stimulate host defense against viruses and tumor cells.<ref>PMID:8034587</ref> <ref>PMID:11146440</ref> <ref>PMID:9501082</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/by/1by2_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/by/1by2_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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=1by2 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 1by2" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Hohenester, E.]]
[[Category: Large Structures]]
[[Category: Sasaki, T.]]
[[Category: Hohenester E]]
[[Category: Timpl, R.]]
[[Category: Sasaki T]]
[[Category: Extracellular matrix]]
[[Category: Timpl R]]
[[Category: Extracellular module]]
[[Category: Glycosylated protein]]
[[Category: Scavenger receptor]]
[[Category: Tumour-associated antigen]]

Latest revision as of 02:50, 21 November 2024

STRUCTURE OF M2BP SCAVENGER RECEPTOR CYSTEINE-RICH DOMAINSTRUCTURE OF M2BP SCAVENGER RECEPTOR CYSTEINE-RICH DOMAIN

Structural highlights

1by2 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
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LG3BP_HUMAN Promotes intergrin-mediated cell adhesion. May stimulate host defense against viruses and tumor cells.[1] [2] [3]

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

Scavenger receptor cysteine-rich (SRCR) domains are found widely in cell surface molecules and in some secreted proteins, where they are thought to mediate ligand binding. We have determined the crystal structure at 2.0 A resolution of the SRCR domain of Mac-2 binding protein (M2BP), a tumor-associated antigen and matrix protein. The structure reveals a curved six-stranded beta-sheet cradling an alpha-helix. Structure-based sequence alignment demonstrates that the M2BP SRCR domain is a valid template for the entire SRCR protein superfamily. This allows an interpretation of previous mutagenesis data on ligand binding to the lymphocyte receptor CD6.

Crystal structure of a scavenger receptor cysteine-rich domain sheds light on an ancient superfamily.,Hohenester E, Sasaki T, Timpl R Nat Struct Biol. 1999 Mar;6(3):228-32. PMID:10074941[4]

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

References

  1. Ullrich A, Sures I, D'Egidio M, Jallal B, Powell TJ, Herbst R, Dreps A, Azam M, Rubinstein M, Natoli C, et al.. The secreted tumor-associated antigen 90K is a potent immune stimulator. J Biol Chem. 1994 Jul 15;269(28):18401-7. PMID:8034587
  2. Tinari N, Kuwabara I, Huflejt ME, Shen PF, Iacobelli S, Liu FT. Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates galectin-1-induced cell aggregation. Int J Cancer. 2001 Jan 15;91(2):167-72. PMID:11146440
  3. Sasaki T, Brakebusch C, Engel J, Timpl R. Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds beta1 integrins, collagens and fibronectin. EMBO J. 1998 Mar 16;17(6):1606-13. PMID:9501082 doi:http://dx.doi.org/10.1093/emboj/17.6.1606
  4. Hohenester E, Sasaki T, Timpl R. Crystal structure of a scavenger receptor cysteine-rich domain sheds light on an ancient superfamily. Nat Struct Biol. 1999 Mar;6(3):228-32. PMID:10074941 doi:http://dx.doi.org/10.1038/6669

1by2, resolution 2.00Å

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OCA