2jsd

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Template:STRUCTURE 2jsd

Contents

Solution structure of MMP20 complexed with NNGH

Template:ABSTRACT PUBMED 17869250

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]

About this Structure

2jsd is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA.

See Also

Reference

  • 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
  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

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