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MMP12 COMPLEX WITH A BETA HYDROXY CARBOXYLIC ACIDMMP12 COMPLEX WITH A BETA HYDROXY CARBOXYLIC ACID
Structural highlights
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 PubMedA new class of selective MMP-12 inhibitors have been identified via high throughput screening. Crystallization with MMP-12 confirmed the mode of binding and allowed initial optimization to be carried out using classical structure based design. The identification of beta-hydroxy carboxylic acids as selective MMP-12 inhibitors.,Holmes IP, Gaines S, Watson SP, Lorthioir O, Walker A, Baddeley SJ, Herbert S, Egan D, Convery MA, Singh OM, Gross JW, Strelow JM, Smith RH, Amour AJ, Brown D, Martin SL Bioorg Med Chem Lett. 2009 Oct 1;19(19):5760-3. Epub 2009 Aug 6. PMID:19703773[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Homo sapiens
- Macrophage elastase
- Amour, A J.
- Baddeley, S J.
- Brown, D.
- Convery, M A.
- Egan, D.
- Gaines, S.
- Gross, J W.
- Herbert, S.
- Holmes, I P.
- Lorthioir, O.
- Martin, S L.
- Singh, O M.P.
- Smith, R H.
- Strelow, J M.
- Walker, A.
- Watson, S P.
- Extracellular matrix
- Glycoprotein
- Hydrolase
- Matrix metalloprotease mmp-12 complex structure
- Metal-binding
- Metalloprotease
- Protease
- Secreted
- Zymogen