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{{STRUCTURE_2jsd| PDB=2jsd |  SCENE=  }}
==Solution structure of MMP20 complexed with NNGH==
===Solution structure of MMP20 complexed with NNGH===
<StructureSection load='2jsd' size='340' side='right' caption='[[2jsd]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
{{ABSTRACT_PUBMED_17869250}}
== Structural highlights ==
<table><tr><td colspan='2'>[[2jsd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JSD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JSD FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NGH:N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL+HYDROXAMIC+ACID'>NGH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MMP20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jsd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jsd RCSB], [http://www.ebi.ac.uk/pdbsum/2jsd PDBsum]</span></td></tr>
<table>
== Disease ==
[[http://www.uniprot.org/uniprot/MMP20_HUMAN MMP20_HUMAN]] Defects in MMP20 are the cause of amelogenesis imperfecta hypomaturation type 2A2 (AI2A2) [MIM:[http://omim.org/entry/612529 612529]]. AI2A2 is an autosomal recessive defect of enamel formation. The disorder involves both primary and secondary dentitions. The teeth have a shiny agar jelly appearance and the enamel is softer than normal. Brown pigment is present in middle layers of enamel.<ref>PMID:15744043</ref>  
== Function ==
[[http://www.uniprot.org/uniprot/MMP20_HUMAN MMP20_HUMAN]] Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation.<ref>PMID:9398237</ref> <ref>PMID:10922468</ref>  
== 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/js/2jsd_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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The solution structure of the catalytic domain of MMP-20, a member of the matrix metalloproteinases family not yet structurally characterized, complexed with N-Isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid (NNGH), is here reported and compared with other MMPs-NNGH adducts. The backbone dynamic has been characterized as well. We have found that, despite the same fold and very high overall similarity, the present structure experiences specific structural and dynamical similarities with some MMPs and differences with others, around the catalytic cavity. The present solution structure, not only contributes to fill the gap of structural knowledge on human MMPs, but also provides further information to design more selective and efficient inhibitors for a specific member of this class of proteins.


==Disease==
Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase.,Arendt Y, Banci L, Bertini I, Cantini F, Cozzi R, Del Conte R, Gonnelli L FEBS Lett. 2007 Oct 2;581(24):4723-6. Epub 2007 Sep 6. PMID:17869250<ref>PMID:17869250</ref>
[[http://www.uniprot.org/uniprot/MMP20_HUMAN MMP20_HUMAN]] Defects in MMP20 are the cause of amelogenesis imperfecta hypomaturation type 2A2 (AI2A2) [MIM:[http://omim.org/entry/612529 612529]]. AI2A2 is an autosomal recessive defect of enamel formation. The disorder involves both primary and secondary dentitions. The teeth have a shiny agar jelly appearance and the enamel is softer than normal. Brown pigment is present in middle layers of enamel.<ref>PMID:15744043</ref>  


==Function==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[http://www.uniprot.org/uniprot/MMP20_HUMAN MMP20_HUMAN]] Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation.<ref>PMID:9398237</ref><ref>PMID:10922468</ref>  
</div>
 
==About this Structure==
[[2jsd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JSD OCA].


==See Also==
==See Also==
*[[Matrix metalloproteinase|Matrix metalloproteinase]]
*[[Matrix metalloproteinase|Matrix metalloproteinase]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:017869250</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Arendt, Y.]]
[[Category: Arendt, Y.]]

Revision as of 11:32, 30 September 2014

Solution structure of MMP20 complexed with NNGHSolution structure of MMP20 complexed with NNGH

Structural highlights

2jsd is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:MMP20 (Homo sapiens)
Resources:FirstGlance, OCA, RCSB, PDBsum

Disease

[MMP20_HUMAN] Defects in MMP20 are the cause of amelogenesis imperfecta hypomaturation type 2A2 (AI2A2) [MIM:612529]. AI2A2 is an autosomal recessive defect of enamel formation. The disorder involves both primary and secondary dentitions. The teeth have a shiny agar jelly appearance and the enamel is softer than normal. Brown pigment is present in middle layers of enamel.[1]

Function

[MMP20_HUMAN] Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation.[2] [3]

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 PubMed

The solution structure of the catalytic domain of MMP-20, a member of the matrix metalloproteinases family not yet structurally characterized, complexed with N-Isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid (NNGH), is here reported and compared with other MMPs-NNGH adducts. The backbone dynamic has been characterized as well. We have found that, despite the same fold and very high overall similarity, the present structure experiences specific structural and dynamical similarities with some MMPs and differences with others, around the catalytic cavity. The present solution structure, not only contributes to fill the gap of structural knowledge on human MMPs, but also provides further information to design more selective and efficient inhibitors for a specific member of this class of proteins.

Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase.,Arendt Y, Banci L, Bertini I, Cantini F, Cozzi R, Del Conte R, Gonnelli L FEBS Lett. 2007 Oct 2;581(24):4723-6. Epub 2007 Sep 6. PMID:17869250[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Kim JW, Simmer JP, Hart TC, Hart PS, Ramaswami MD, Bartlett JD, Hu JC. MMP-20 mutation in autosomal recessive pigmented hypomaturation amelogenesis imperfecta. J Med Genet. 2005 Mar;42(3):271-5. PMID:15744043 doi:10.1136/jmg.2004.024505
  2. ↑ Llano E, Pendas AM, Knauper V, Sorsa T, Salo T, Salido E, Murphy G, Simmer JP, Bartlett JD, Lopez-Otin C. Identification and structural and functional characterization of human enamelysin (MMP-20). Biochemistry. 1997 Dec 9;36(49):15101-8. PMID:9398237 doi:10.1021/bi972120y
  3. ↑ Stracke JO, Fosang AJ, Last K, Mercuri FA, Pendas AM, Llano E, Perris R, Di Cesare PE, Murphy G, Knauper V. Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP). FEBS Lett. 2000 Jul 28;478(1-2):52-6. PMID:10922468
  4. ↑ Arendt Y, Banci L, Bertini I, Cantini F, Cozzi R, Del Conte R, Gonnelli L. Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase. FEBS Lett. 2007 Oct 2;581(24):4723-6. Epub 2007 Sep 6. PMID:17869250 doi:10.1016/j.febslet.2007.08.069
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