2jsd

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.
Method:	Solution NMR
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

References

↑ 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
↑ 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
↑ 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
↑ 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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OCA

[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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2jsd

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

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

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2jsd

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

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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