Human stromelysin

Winyard, P.G., Zhang, Z., Chidwick, K., Blake, D.R., Carrell, R.W. and Murphy, G. (1991). Proteolytic inactivation of human ai-antitrypsin by human stromelysin. FEES Lett. 279, 91-93. 

Three-Dimensional Structure of the Inhibited Catalytic Domain of Human Stromelysin-1 by Heteronuclear NMR Spectroscopy... 

Gooley PR, O Connell JF, Marcy AI, Cuca GC, Salowe SP, Bush BL, Hermes JD, Hagmann WK, Esser CK, Springer JP, Johnson BA. The NMR structure of the inhibited catalytic domain of human stromelysin-1. Nat Struct Biol 1994 1 111-118. 

Van Doren SR, Kurochkin AV, Hu W, Ye Q-Z, Johnson LL, Hupe DJ, Zuiderweg ERP. Solution structure of the catalytic domain of human stromelysin complexed with a hydrophobic inhibitor. Prot Sci 1995 4 2487-2498. 

A common way to benefit from the ability to combine different molecular orbital methods in ONIOM is to combine a DFT or ab-initio description of the reactive region with a semi-empirical treatment of the immediate protein environment, including up to 1000 atoms. Due to the requirement for reliable semi-empirical parameters, as discussed in Section 2.2.1, this approach has primarily been used for non-metal or Zn-enzymes. Examples include human stromelysin-1 [83], carboxypeptidase [84], ribonucleotide reductase (substrate reaction) [85], farnesyl transferase [86] and cytosine deaminase [87], Combining two ab-initio methods of different accuracy is not common in biocatalysis applications, and one example from is an ONIOM (MP2 HF) study of catechol O-methyltransferase [88],... 

Inhibitors of human neutrophil collagenase and human stromelysin have been designed (577) which are based on previous classes of MMP inhibitors, iV-carboxyalkyl peptides (578, 579), and peptide-based hy-droxamic acids (117) (580, 581). The -CH3 and 2-phenylethyl groups are important for inhibition of MMP-3. The X-ray crystal structure of MMP-3 with bound 117 shows that the inhibitor chelates Zn(II)... 

MMP-2) Human stromelysin-1 (MMP-3) 2SRT, 1BM6 HiSa 3 HiSa 5 His H2O ... 

Ahmad, A., Marshall, J. F., Basset, R, Anglard, P. and Hart, I. R. (1997). Modulation of human stromelysin 3 promoter activity and gene expression by human breast cancer cells. Int. J. Cancer 73, 290-296. 

Drug Discovery Strategies and Methods, ed. A. Makriyannis and D. Biegel, Marcel Dekker, Inc., New York, N.Y., 2004 R 186 P.R. Gooley, Three-Dimensional Structure of the Inhibited Catalytic Domain of Human Stromelysin-1 by Heteronuclear NMR Spectroscopy , p. 61... 

Examples of the application of SAR-by-NMR include the design of stromelysin and human papillomavirus E2 protein inhibitors [7, 8]. 

Marcy AI, Eiberger LL, Harrison R, Chan HK, Hutchinson NI, Hagmann WK, Cameron PM, Boulton DA, Hermes JD. Human fibroblast stromelysin catalytic domain expression, purification and characterization of a C-terminally truncated form. Biochemistry 1991 30 6476-6483. 

Stromelysin was isolated as the zymogen from the culture media of interleukin-1-stimulated human gingival fibroblasts. The zymogen is activated by incubating with trypsin, which in turn is inactivated by adding soybean trypsin inhibitor. 

Shapiro, S.D., Campbell, E.J., Kobayashi, D.K and Welgus, H.G. (1991). Immune modulation of metalloproteinase production in human macrophages. Selective pretranslational suppression of interstitial coUagenase and stromelysin biosynthesis by interferon-gamma. J. Clin. Invest. 88, 1656-1662. 

Obata, K., Iwata, K., Okada, Y., et al., A one-step sandwich enzyme immunoassay for human matrix metalloproteinase 3 (stromelysin-1) using monoclonal antibodies. Clin. Chim. Acta 211, 59-72 (1992). 

Stromelysin 3 (= matrix metalloproteinase 11) from rat skin has 491 amino acids, and shows 83,95 and 58 % homology with human, mouse and Xeno-pus ST3, respectively (Okada et al. 1997). In contrast to other matrix metalloproteinases, ST3 is secreted into the extracellular space as a potentially active molecule (Pei and Weiss 1995, Santavicca et al. 1996). By in situ hybridisation. Wolf et al. (1993) detected ST3 transcripts specifically in fibroblastic cells in primary breast carcinomas and so did Okada et al. (1997) in fibroblastic cells loca-hsed in the superficial dermis of healing rat skin wounds. 

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