3edi: Difference between revisions
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== | ==Crystal structure of tolloid-like protease 1 (TLL-1) protease domain== | ||
[[http://www.uniprot.org/uniprot/TLL1_HUMAN TLL1_HUMAN | <StructureSection load='3edi' size='340' side='right'caption='[[3edi]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3edi]] 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=3EDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EDI 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]] 1.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=3edi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edi OCA], [https://pdbe.org/3edi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3edi RCSB], [https://www.ebi.ac.uk/pdbsum/3edi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3edi ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/TLL1_HUMAN TLL1_HUMAN] Defects in TLL1 are the cause of atrial septal defect type 6 (ASD6) [MIM:[https://omim.org/entry/613087 613087]. A congenital heart malformation characterized by incomplete closure of the wall between the atria resulting in blood flow from the left to the right atria.<ref>PMID:18830233</ref> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TLL1_HUMAN TLL1_HUMAN] Protease which processes procollagen C-propeptides, such as chordin, pro-biglycan and pro-lysyl oxidase. Required for the embryonic development. Predominant protease, which in the development, influences dorsal-ventral patterning and skeletogenesis. | |||
== 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/ed/3edi_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=3edi ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Procollagen C-peptidase, also known as bone morphogenetic protein 1 (BMP-1), is a multidomain, zinc endopeptidase of the astacin M12A family. BMP-1 is the prototype of a small group of proteases that have key roles in extracellular matrix formation and morphogenesis. BMP-1, its splice form mTLD, and the related proteases TLL-1 and TLL-2 are considered as promising drug targets for the treatment of excessive fibrosis and muscle wasting. We report here the crystal structures of the protease domains of human BMP-1 and the closely related Tolloid-like protease 1 (TLL-1). The crystal structures reveal an unexpected conformation of a cysteine-rich loop within the active site, and suggest that a flap movement is required in order to allow substrate binding. On the basis of these substantial differences between the BMP-1 and astacin active sites, a structural basis for their differing substrate specificities is proposed. | |||
Structural basis for the substrate specificity of bone morphogenetic protein 1/tolloid-like metalloproteases.,Mac Sweeney A, Gil-Parrado S, Vinzenz D, Bernardi A, Hein A, Bodendorf U, Erbel P, Logel C, Gerhartz B J Mol Biol. 2008 Dec 5;384(1):228-39. doi: 10.1016/j.jmb.2008.09.029. Epub 2008 , Sep 19. PMID:18824173<ref>PMID:18824173</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3edi" style="background-color:#fffaf0;"></div> | |||
== | == References == | ||
<references | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mac Sweeney A]] | ||
Latest revision as of 18:20, 1 November 2023
Crystal structure of tolloid-like protease 1 (TLL-1) protease domainCrystal structure of tolloid-like protease 1 (TLL-1) protease domain
Structural highlights
DiseaseTLL1_HUMAN Defects in TLL1 are the cause of atrial septal defect type 6 (ASD6) [MIM:613087. A congenital heart malformation characterized by incomplete closure of the wall between the atria resulting in blood flow from the left to the right atria.[1] FunctionTLL1_HUMAN Protease which processes procollagen C-propeptides, such as chordin, pro-biglycan and pro-lysyl oxidase. Required for the embryonic development. Predominant protease, which in the development, influences dorsal-ventral patterning and skeletogenesis. 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 PubMedProcollagen C-peptidase, also known as bone morphogenetic protein 1 (BMP-1), is a multidomain, zinc endopeptidase of the astacin M12A family. BMP-1 is the prototype of a small group of proteases that have key roles in extracellular matrix formation and morphogenesis. BMP-1, its splice form mTLD, and the related proteases TLL-1 and TLL-2 are considered as promising drug targets for the treatment of excessive fibrosis and muscle wasting. We report here the crystal structures of the protease domains of human BMP-1 and the closely related Tolloid-like protease 1 (TLL-1). The crystal structures reveal an unexpected conformation of a cysteine-rich loop within the active site, and suggest that a flap movement is required in order to allow substrate binding. On the basis of these substantial differences between the BMP-1 and astacin active sites, a structural basis for their differing substrate specificities is proposed. Structural basis for the substrate specificity of bone morphogenetic protein 1/tolloid-like metalloproteases.,Mac Sweeney A, Gil-Parrado S, Vinzenz D, Bernardi A, Hein A, Bodendorf U, Erbel P, Logel C, Gerhartz B J Mol Biol. 2008 Dec 5;384(1):228-39. doi: 10.1016/j.jmb.2008.09.029. Epub 2008 , Sep 19. PMID:18824173[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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