1edy: Difference between revisions

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{{Seed}}
[[Image:1edy.png|left|200px]]


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==CRYSTAL STRUCTURE OF RAT ALPHA 1-MACROGLOBULIN RECEPTOR BINDING DOMAIN==
The line below this paragraph, containing "STRUCTURE_1edy", creates the "Structure Box" on the page.
<StructureSection load='1edy' size='340' side='right'caption='[[1edy]], [[Resolution|resolution]] 2.30&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'>[[1edy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EDY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EDY FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=1edy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1edy OCA], [https://pdbe.org/1edy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1edy RCSB], [https://www.ebi.ac.uk/pdbsum/1edy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1edy ProSAT]</span></td></tr>
{{STRUCTURE_1edy|  PDB=1edy  |  SCENE=  }}
</table>
 
== Function ==
===CRYSTAL STRUCTURE OF RAT ALPHA 1-MACROGLOBULIN RECEPTOR BINDING DOMAIN===
[https://www.uniprot.org/uniprot/A1M_RAT A1M_RAT] 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).[UniProtKB:P01023]
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ed/1edy_consurf.spt"</scriptWhenChecked>
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==About this Structure==
</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=1edy ConSurf].
1EDY is a 2 chains structure of sequences 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=1EDY OCA].  
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__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:11106161</ref><references group="xtra"/>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: DeCamp, D L.]]
[[Category: DeCamp DL]]
[[Category: Sprang, S R.]]
[[Category: Sprang SR]]
[[Category: Xiao, T.]]
[[Category: Xiao T]]
[[Category: Beta sandwich]]
[[Category: Pseudo-symmetric dimer]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 14:18:18 2009''

Latest revision as of 10:01, 7 February 2024

CRYSTAL STRUCTURE OF RAT ALPHA 1-MACROGLOBULIN RECEPTOR BINDING DOMAINCRYSTAL STRUCTURE OF RAT ALPHA 1-MACROGLOBULIN RECEPTOR BINDING DOMAIN

Structural highlights

1edy is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A1M_RAT 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).[UniProtKB:P01023]

Evolutionary Conservation

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

1edy, resolution 2.30Å

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OCA
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