3.4.24.34: neutrophil collagenase
This is an abbreviated version!
For detailed information about neutrophil collagenase, go to the full flat file.
Word Map on EC 3.4.24.34
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3.4.24.34
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mmp-9
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metalloproteinases
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zymography
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metastasis
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timp-1
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endothelial
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angiogenesis
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necrosis
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artery
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fibrosis
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cartilage
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gelatinase
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gelatin
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osteoarthritis
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joint
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periodontal
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tnf
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arthritis
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plaque
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infarct
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vessel
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rheumatoid
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myocardial
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invasiveness
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plasminogen
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basement
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synovial
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chondrocytes
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gingival
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articular
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transwell
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mt1-mmp
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aortic
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aneurysm
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collagenolytic
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aggrecan
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matrigel
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atherosclerotic
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stromelysins
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signal-regulated
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erk
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crevicular
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doxycycline
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gelatinolytic
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matrix-degrading
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anti-invasive
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diagnostics
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disintegrin
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upa
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photoaging
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membrane-type
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medicine
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biotechnology
- 3.4.24.34
- mmp-9
- metalloproteinases
-
zymography
- metastasis
- timp-1
- endothelial
- angiogenesis
- necrosis
- artery
- fibrosis
- cartilage
- gelatinase
- gelatin
- osteoarthritis
- joint
- periodontal
- tnf
- arthritis
- plaque
- infarct
- vessel
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rheumatoid
- myocardial
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invasiveness
- plasminogen
-
basement
- synovial
- chondrocytes
- gingival
-
articular
-
transwell
- mt1-mmp
- aortic
- aneurysm
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collagenolytic
- aggrecan
- matrigel
- atherosclerotic
- stromelysins
-
signal-regulated
- erk
-
crevicular
- doxycycline
-
gelatinolytic
-
matrix-degrading
-
anti-invasive
- diagnostics
-
disintegrin
- upa
-
photoaging
-
membrane-type
- medicine
- biotechnology
Reaction
Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, interstitial collagenase, this enzyme cleaves type III collagen additional information slowly than type I =
Synonyms
collagenase-2, collagenases-8, EC 3.4.24.7, HNC, human neutrophil collagenase, matrix metalloproteinase, Matrix metalloproteinase 8, Matrix metalloproteinase-8, metalloproteinase-8, MetMMP-8, MMP-7, MMP-8, MMP8, neutrophil collagenase, neutrophil collagenase MMP-8, neutrophil interstitial collagenase, PheMMP-8, PMNL collagenase, PMNL-CL, polymorphonuclear leukocyte collagenase, whMMP-8
ECTree
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Crystallization
Crystallization on EC 3.4.24.34 - neutrophil collagenase
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crystal structure of the catalytic domain in non-covalent complex with the hydroxamate inhibitor BB-1909, space group P2(1)2(1)2(1), cell constants a : 4.47 nm, b : 8.08 nm, c : 10.81 nm
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crystallized using hanging drop method, space group P2(1)2(1)2(1), cell dimesions a : 33.1 A, b : 68.9 A, c : 70.5 A
in complex with a primed and an unprimed-side inhibitor, hanging-drop vapor diffusion, space group P2(1)2(1)2(1), cell dimensions a : 32.98 A, b : 68.67 A, c : 70.49 A
in complex with inhibitor HONH-iBM-L-Ala-Gly-NH2, vapor-diffusion technique, hanging drop
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MMP-8 in complex with inhibitors (S)- and (R)-alpha-arylsulfonylamino phosphonate, hanging drop vapor diffusion method at 18°C, mixing of 0.0015 ml of protein solution containing 6 mg/mL protein in 5 mM CaCl2, 100 mM NaCl, 0.5 mM ZnCl2, 3 mM MES-NaOH, 0.02% NaN3, pH 6.0, with 0.001 ml of inhibitor solution containing 1 mM inhibitor in 0.2 M MES-NaOH, 20% MeOH, pH 6.0, and 0.005 ml of PEG solution containing 10% m/v PEG 6000, 0.2 M MES-NaOH, 0.02% NaN3, pH 6.0, droplets are concentrated against a reservoir buffer containing 1.6 M sodium phosphate buffer, 0.02% NaN3, pH 6.0, X-ray diffraction structure determination and anaylsis at 1.56-1.94 A resolution
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