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3edh
From Proteopedia
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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]] 1.25Å' scene=''> | + | <StructureSection load='3edh' size='340' side='right'caption='[[3edh]], [[Resolution|resolution]] 1.25Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3edh]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3edh]] 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=3EDH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EDH 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=DMS:DIMETHYL+SULFOXIDE'>DMS</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=DMS:DIMETHYL+SULFOXIDE'>DMS</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">[[3edg|3edg]], [[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;'>[[3edg|3edg]], [[3edi|3edi]], [[1dle|1dle]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BMP1, PCOLC ([ | + | <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'>[ | + | <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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3edh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edh OCA], [https://pdbe.org/3edh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3edh RCSB], [https://www.ebi.ac.uk/pdbsum/3edh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3edh ProSAT]</span></td></tr> |
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | [[ | + | [[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 == | ||
| - | [[ | + | [[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 11:47, 16 February 2022
Crystal structure of bone morphogenetic protein 1 protease domain in complex with partially bound DMSO
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Categories: Human | Large Structures | Procollagen C-endopeptidase | Sweeney, A Mac | Alternative splicing | Calcium | Chondrogenesis | Cleavage on pair of basic residue | Cytokine | Developmental protein | Differentiation | Egf-like domain | Glycoprotein | Growth factor | Hydrolase | Metal-binding | Metalloprotease | Osteogenesis | Polymorphism | Protease | Vicinal disulfide | Zinc | Zymogen

