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Literature DB >> 24637763

Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of membrane type 1 matrix metalloproteinase.

Hideaki Ogata¹, Elena Decaneto¹, Moran Grossman², Martina Havenith², Irit Sagi³, Wolfgang Lubitz¹, Markus Knipp¹.

Abstract

Membrane type 1 matrix metalloproteinase (MT1-MMP) belongs to the large family of zinc-dependent endopeptidases termed MMPs that are located in the extracellular matrix. MT1-MMP was crystallized at 277 K using the vapour-diffusion method with PEG as a precipitating agent. Data sets for MT1-MMP were collected to 2.24 Å resolution at 100 K. The crystals belonged to space group P4(3)2(1)2, with unit-cell parameters a = 62.99, c = 122.60 Å. The crystal contained one molecule per asymmetric unit, with a Matthews coefficient (VM) of 2.90 Å(3) Da(-1); the solvent content is estimated to be 57.6%.

Entities: Chemical Gene

Keywords: membrane type 1 matrix metalloproteinase

Mesh：

Substances：

Year: 2014 PMID： 24637763 PMCID： PMC3936455 DOI： 10.1107/S2053230X13034857

Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN： 2053-230X Impact factor: 1.056

17 in total

Review 1. Matrix metalloproteinases.

Authors: H Nagase; J F Woessner
Journal: J Biol Chem Date: 1999-07-30 Impact factor: 5.157

2. Snapshots of the reaction mechanism of matrix metalloproteinases.

Authors: Ivano Bertini; Vito Calderone; Marco Fragai; Claudio Luchinat; Massimiliano Maletta; Kwon Joo Yeo
Journal: Angew Chem Int Ed Engl Date: 2006-12-04 Impact factor: 15.336

Review 3. Matrix metalloproteinases: fold and function of their catalytic domains.

Authors: Cynthia Tallant; Aniebrys Marrero; F Xavier Gomis-Rüth
Journal: Biochim Biophys Acta Date: 2009-04-15

Review 4. Progress in matrix metalloproteinase research.

Authors: Gillian Murphy; Hideaki Nagase
Journal: Mol Aspects Med Date: 2008-05-24

5. Molecular replacement with MOLREP.

Authors: Alexei Vagin; Alexei Teplyakov
Journal: Acta Crystallogr D Biol Crystallogr Date: 2009-12-21

6. XDS.

Authors: Wolfgang Kabsch
Journal: Acta Crystallogr D Biol Crystallogr Date: 2010-01-22

7. Solvent content of protein crystals.

Authors: B W Matthews
Journal: J Mol Biol Date: 1968-04-28 Impact factor: 5.469

8. The intrinsic protein flexibility of endogenous protease inhibitor TIMP-1 controls its binding interface and affects its function.

Authors: Moran Grossman; Dmitry Tworowski; Orly Dym; Meng-Huee Lee; Yaakov Levy; Gillian Murphy; Irit Sagi
Journal: Biochemistry Date: 2010-07-27 Impact factor: 3.162

9. X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: implications for inhibitor selectivity.

Authors: A G Pavlovsky; M G Williams; Q Z Ye; D F Ortwine; C F Purchase; A D White; V Dhanaraj; B D Roth; L L Johnson; D Hupe; C Humblet; T L Blundell
Journal: Protein Sci Date: 1999-07 Impact factor: 6.725

10. Characterization of Mca-Lys-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2, a fluorogenic substrate with increased specificity constants for collagenases and tumor necrosis factor converting enzyme.

Authors: Ulf Neumann; Hisashi Kubota; Karl Frei; Vishwas Ganu; David Leppert
Journal: Anal Biochem Date: 2004-05-15 Impact factor: 3.365

7 in total

1. Development of High Affinity and High Specificity Inhibitors of Matrix Metalloproteinase 14 through Computational Design and Directed Evolution.

Authors: Valeria Arkadash; Gal Yosef; Jason Shirian; Itay Cohen; Yuval Horev; Moran Grossman; Irit Sagi; Evette S Radisky; Julia M Shifman; Niv Papo
Journal: J Biol Chem Date: 2017-01-13 Impact factor: 5.157

Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of membrane type 1 matrix metalloproteinase.

Review 1. Matrix metalloproteinases.

2. Snapshots of the reaction mechanism of matrix metalloproteinases.

Review 3. Matrix metalloproteinases: fold and function of their catalytic domains.

Review 4. Progress in matrix metalloproteinase research.

5. Molecular replacement with MOLREP.

6. XDS.

7. Solvent content of protein crystals.

8. The intrinsic protein flexibility of endogenous protease inhibitor TIMP-1 controls its binding interface and affects its function.

9. X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: implications for inhibitor selectivity.

10. Characterization of Mca-Lys-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2, a fluorogenic substrate with increased specificity constants for collagenases and tumor necrosis factor converting enzyme.

1. Development of High Affinity and High Specificity Inhibitors of Matrix Metalloproteinase 14 through Computational Design and Directed Evolution.

2. Targeting the MMP-14/MMP-2/integrin α_vβ₃ axis with multispecific N-TIMP2-based antagonists for cancer therapy.

3. Quantitative mapping of binding specificity landscapes for homologous targets by using a high-throughput method.

4. Pressure and Temperature Effects on the Activity and Structure of the Catalytic Domain of Human MT1-MMP.

5. Combinatorial engineering of N-TIMP2 variants that selectively inhibit MMP9 and MMP14 function in the cell.

Review 6. Developments in Carbohydrate-Based Metzincin Inhibitors.

7. Local Mutations Can Serve as a Game Changer for Global Protein Solvent Interaction.