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==Crystal structure of bone morphogenetic protein 1 protease domain==
==Crystal structure of bone morphogenetic protein 1 protease domain==
<StructureSection load='3edg' size='340' side='right' caption='[[3edg]], [[Resolution|resolution]] 1.27&Aring;' scene=''>
<StructureSection load='3edg' size='340' side='right'caption='[[3edg]], [[Resolution|resolution]] 1.27&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3edg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EDG FirstGlance]. <br>
<table><tr><td colspan='2'>[[3edg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EDG FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</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=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3edh|3edh]], [[3edi|3edi]], [[1dle|1dle]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3edh|3edh]], [[3edi|3edi]], [[1dle|1dle]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BMP1, PCOLC ([https://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'>[https://en.wikipedia.org/wiki/Procollagen_C-endopeptidase Procollagen C-endopeptidase], with EC number [https://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=3edg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edg OCA], [http://pdbe.org/3edg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3edg RCSB], [http://www.ebi.ac.uk/pdbsum/3edg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3edg ProSAT]</span></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=3edg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edg OCA], [https://pdbe.org/3edg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3edg RCSB], [https://www.ebi.ac.uk/pdbsum/3edg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3edg ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/BMP1_HUMAN BMP1_HUMAN]] Defects in BMP1 are the cause of osteogenesis imperfecta 13 (OI13) [MIM:[http://omim.org/entry/614856 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.<ref>PMID:22482805</ref> <ref>PMID:22052668</ref>   
[[https://www.uniprot.org/uniprot/BMP1_HUMAN BMP1_HUMAN]] Defects in BMP1 are the cause of osteogenesis imperfecta 13 (OI13) [MIM:[https://omim.org/entry/614856 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.<ref>PMID:22482805</ref> <ref>PMID:22052668</ref>   
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/BMP1_HUMAN 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.  
[[https://www.uniprot.org/uniprot/BMP1_HUMAN 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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[Bone morphogenetic protein|Bone morphogenetic protein]]
*[[Bone morphogenetic protein 3D structures|Bone morphogenetic protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Procollagen C-endopeptidase]]
[[Category: Procollagen C-endopeptidase]]
[[Category: Sweeney, A Mac]]
[[Category: Sweeney, A Mac]]

Revision as of 14:47, 16 February 2022

Crystal structure of bone morphogenetic protein 1 protease domainCrystal structure of bone morphogenetic protein 1 protease domain

Structural highlights

3edg 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

3edg, resolution 1.27Å

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