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[[Image:1ayo.gif|left|200px]]<br />
<applet load="1ayo" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ayo, resolution 1.90&Aring;" />
'''RECEPTOR BINDING DOMAIN OF BOVINE ALPHA-2-MACROGLOBULIN'''<br />


==Overview==
==RECEPTOR BINDING DOMAIN OF BOVINE ALPHA-2-MACROGLOBULIN==
BACKGROUND: The large plasma proteinase inhibitors of the alpha, 2-macroglobulin superfamily inhibit proteinases by capturing them within a, central cavity of the inhibitor molecule. After reaction with the, proteinase, the alpha-macroglobulin-proteinase complex binds to the, alpha-macroglobulin receptor, present in the liver and other tissues, and, becomes endocytosed and rapidly removed from the circulation. The complex, binds to the receptor via recognition sites located on a separate domain, of approximately 138 residues positioned at the C terminus of the, alpha-macroglobulin subunit. RESULTS: The crystal structure of the, receptor-binding domain of bovine alpha 2-macroglobulin (bRBD) has been, determined at a resolution of 1.9 A. The domain primarily comprises a, nine-strand beta ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9634697 (full description)]]
<StructureSection load='1ayo' size='340' side='right'caption='[[1ayo]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1ayo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AYO FirstGlance]. <br>
1AYO is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Sites: S1 and S2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AYO OCA]].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ayo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ayo OCA], [https://pdbe.org/1ayo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ayo RCSB], [https://www.ebi.ac.uk/pdbsum/1ayo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ayo ProSAT]</span></td></tr>
Crystal structure of the receptor-binding domain of alpha 2-macroglobulin., Jenner L, Husted L, Thirup S, Sottrup-Jensen L, Nyborg J, Structure. 1998 May 15;6(5):595-604. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9634697 9634697]
</table>
== Function ==
[https://www.uniprot.org/uniprot/A2MG_BOVIN A2MG_BOVIN] Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase (By similarity).
== 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/ay/1ayo_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=1ayo ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Husted, L.]]
[[Category: Husted L]]
[[Category: Jenner, L.B.]]
[[Category: Jenner LB]]
[[Category: Nyborg, J.]]
[[Category: Nyborg J]]
[[Category: Sottrup-Jensen, L.]]
[[Category: Sottrup-Jensen L]]
[[Category: Thirup, S.]]
[[Category: Thirup S]]
[[Category: CA]]
[[Category: macroglobulin]]
[[Category: receptor binding domain]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:52:57 2007''

Latest revision as of 18:29, 13 March 2024

RECEPTOR BINDING DOMAIN OF BOVINE ALPHA-2-MACROGLOBULINRECEPTOR BINDING DOMAIN OF BOVINE ALPHA-2-MACROGLOBULIN

Structural highlights

1ayo is a 2 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A2MG_BOVIN Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase (By similarity).

Evolutionary Conservation

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

1ayo, resolution 1.90Å

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