3edh

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{{STRUCTURE_3edh| PDB=3edh | SCENE= }}
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==Crystal structure of bone morphogenetic protein 1 protease domain in complex with partially bound DMSO==
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===Crystal structure of bone morphogenetic protein 1 protease domain in complex with partially bound DMSO===
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<StructureSection load='3edh' size='340' side='right' caption='[[3edh]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
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== Structural highlights ==
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==Disease==
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<table><tr><td colspan='2'>[[3edh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EDH FirstGlance]. <br>
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[[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>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3edg|3edg]], [[3edi|3edi]], [[1dle|1dle]]</td></tr>
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==Function==
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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 Homo sapiens])</td></tr>
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<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>
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<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://www.rcsb.org/pdb/explore.do?structureId=3edh RCSB], [http://www.ebi.ac.uk/pdbsum/3edh PDBsum]</span></td></tr>
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</table>
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== Disease ==
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[[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>
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== 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.
[[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.
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== Evolutionary Conservation ==
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==About this Structure==
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[[Image:Consurf_key_small.gif|200px|right]]
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[[3edh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDH OCA].
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Check<jmol>
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<jmolCheckbox>
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==Reference==
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ed/3edh_consurf.spt"</scriptWhenChecked>
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<references group="xtra"/><references/>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Procollagen C-endopeptidase]]
[[Category: Procollagen C-endopeptidase]]
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[[Category: Sweeney, A Mac.]]
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[[Category: Sweeney, A Mac]]
[[Category: Chondrogenesis]]
[[Category: Chondrogenesis]]
[[Category: Cleavage on pair of basic residue]]
[[Category: Cleavage on pair of basic residue]]

Revision as of 14:06, 18 December 2014

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

3edh, resolution 1.25Å

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