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==Crystal structure of bone morphogenetic protein 1 protease domain in complex with partially bound DMSO==
==Crystal structure of bone morphogenetic protein 1 protease domain in complex with partially bound DMSO==
<StructureSection load='3edh' size='340' side='right' caption='[[3edh]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
<StructureSection load='3edh' size='340' side='right' caption='[[3edh]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BMP1, PCOLC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BMP1, PCOLC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Procollagen_C-endopeptidase Procollagen C-endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.19 3.4.24.19] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Procollagen_C-endopeptidase Procollagen C-endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.19 3.4.24.19] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3edh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edh OCA], [http://pdbe.org/3edh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3edh RCSB], [http://www.ebi.ac.uk/pdbsum/3edh PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3edh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edh OCA], [http://pdbe.org/3edh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3edh RCSB], [http://www.ebi.ac.uk/pdbsum/3edh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3edh ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ed/3edh_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ed/3edh_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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</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=3edh 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=3edh ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
==See Also==
*[[Bone morphogenetic protein|Bone morphogenetic protein]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Procollagen C-endopeptidase]]
[[Category: Procollagen C-endopeptidase]]
[[Category: Sweeney, A Mac]]
[[Category: Sweeney, A Mac]]
[[Category: Alternative splicing]]
[[Category: Calcium]]
[[Category: Chondrogenesis]]
[[Category: Chondrogenesis]]
[[Category: Cleavage on pair of basic residue]]
[[Category: Cleavage on pair of basic residue]]
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[[Category: Metalloprotease]]
[[Category: Metalloprotease]]
[[Category: Osteogenesis]]
[[Category: Osteogenesis]]
[[Category: Polymorphism]]
[[Category: Protease]]
[[Category: Protease]]
[[Category: Vicinal disulfide]]
[[Category: Vicinal disulfide]]
[[Category: Zinc]]
[[Category: Zymogen]]
[[Category: Zymogen]]

Revision as of 00:59, 3 December 2018

Crystal structure of bone morphogenetic protein 1 protease domain in complex with partially bound DMSOCrystal structure of bone morphogenetic protein 1 protease domain in complex with partially bound DMSO

Structural highlights

3edh 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.
Ligands:, ,
Gene:BMP1, PCOLC (HUMAN)
Activity:Procollagen C-endopeptidase, with EC number 3.4.24.19
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[BMP1_HUMAN] Defects in BMP1 are the cause of osteogenesis imperfecta 13 (OI13) [MIM:614856]. An autosomal recessive form of osteogenesis imperfecta, a connective tissue disorder characterized by bone fragility, low bone mass, and recurrent fractures. OI13 is characterized by normal teeth, faint blue sclerae, severe growth deficiency, borderline osteoporosis, severe bone deformity, and recurrent fractures affecting both upper and lower limbs.[1] [2]

Function

[BMP1_HUMAN] Cleaves the C-terminal propeptides of procollagen I, II and III. Induces cartilage and bone formation. May participate in dorsoventral patterning during early development by cleaving chordin (CHRD). Responsible for the proteolytic activation of lysyl oxidase LOX.

Evolutionary Conservation

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

See Also

References

  1. ↑ Asharani PV, Keupp K, Semler O, Wang W, Li Y, Thiele H, Yigit G, Pohl E, Becker J, Frommolt P, Sonntag C, Altmuller J, Zimmermann K, Greenspan DS, Akarsu NA, Netzer C, Schonau E, Wirth R, Hammerschmidt M, Nurnberg P, Wollnik B, Carney TJ. Attenuated BMP1 function compromises osteogenesis, leading to bone fragility in humans and zebrafish. Am J Hum Genet. 2012 Apr 6;90(4):661-74. doi: 10.1016/j.ajhg.2012.02.026. PMID:22482805 doi:10.1016/j.ajhg.2012.02.026
  2. ↑ Martinez-Glez V, Valencia M, Caparros-Martin JA, Aglan M, Temtamy S, Tenorio J, Pulido V, Lindert U, Rohrbach M, Eyre D, Giunta C, Lapunzina P, Ruiz-Perez VL. Identification of a mutation causing deficient BMP1/mTLD proteolytic activity in autosomal recessive osteogenesis imperfecta. Hum Mutat. 2012 Feb;33(2):343-50. doi: 10.1002/humu.21647. Epub 2011 Nov 30. PMID:22052668 doi:10.1002/humu.21647

3edh, resolution 1.25Å

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