Neutrophil collagenase

Function

Can degrade fibrillar type I, II, and III collagens.

Classification

Family (Pfam)

PF00045 Hemopexin, PF00413 Peptidase_M10, PF01471 PG_binding_1

InterPro

Hemopexin-like_dom, Hemopexin-like_dom_sf, Hemopexin-like_repeat, Hemopexin_CS, M10A_MMP, MetalloPept_cat_dom_sf, Pept_M10_metallopeptidase, Pept_M10A, Pept_M10A_Zn_BS, Peptidase_Metallo, Peptidoglycan-bd-like, PGBD-like_sf

Functional cluster

Venom Serine Proteases & Phospholipase A2

Experimental structures · PDB · 25

• 1A85 X-ray 2.00A
• 1A86 X-ray 2.00A
• 1BZS X-ray 1.70A
• 1I73 X-ray 1.40A
• 1I76 X-ray 1.20A
• 1JAN X-ray 2.50A
• 1JAO X-ray 2.40A
• 1JAP X-ray 1.82A
• 1JAQ X-ray 2.40A
• 1JH1 X-ray 2.70A
• 1JJ9 X-ray 2.00A
• 1KBC X-ray 1.80A
• … and 13 more

A predicted model is available from AlphaFold.

Gene Ontology · 21

• GO:0031012 extracellular matrix
• GO:0005576 extracellular region
• GO:0005615 extracellular space
• GO:0035580 specific granule lumen
• GO:1904724 tertiary granule lumen
• GO:0004175 endopeptidase activity
• GO:0004222 metalloendopeptidase activity
• GO:0008233 peptidase activity
• GO:0004252 serine-type endopeptidase activity
• GO:0043120 tumor necrosis factor binding
• GO:0008270 zinc ion binding
• GO:0071222 cellular response to lipopolysaccharide
• GO:0030574 collagen catabolic process
• GO:0035987 endodermal cell differentiation
• GO:0022617 extracellular matrix disassembly
• GO:0030198 extracellular matrix organization
• GO:1903980 positive regulation of microglial cell activation
• GO:0150078 positive regulation of neuroinflammatory response
• GO:0032760 positive regulation of tumor necrosis factor production
• GO:1903265 positive regulation of tumor necrosis factor-mediated signaling pathway
• GO:0006508 proteolysis

Drugs targeting this protein · 5

• DOXYCYCLINE inhibitor
• DOXYCYCLINE CALCIUM inhibitor
• DOXYCYCLINE HYCLATE inhibitor
• CTS-1027 inhibitor
• REBIMASTAT inhibitor

Related proteins · sequence + function similarity

• Neutrophil collagenase 0.96
• Neutrophil collagenase 0.96
• Interstitial collagenase 0.92
• Matrix metalloproteinase-18 0.92
• Interstitial collagenase 0.92
• Interstitial collagenase 0.92
• Interstitial collagenase 0.91
• Stromelysin-1 0.90
• Interstitial collagenase A 0.90
• Macrophage metalloelastase 0.90
• Interstitial collagenase 0.89
• Stromelysin-1 0.88

Literature · 13 cited papers

• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. · 2004
• Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data. Protein Sci. · 1998
• 1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile. Eur. J. Biochem. · 1997
• Structural implications for the role of the N-terminus in the 'superactivation' of collagenases. A crystallographic study. FEBS Lett. · 1994
• The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity. EMBO J. · 1994
• Structure of human neutrophil collagenase reveals large S1' specificity pocket. Nat. Struct. Biol. · 1994
• Characterization of 58-kilodalton human neutrophil collagenase: comparison with human fibroblast collagenase. Biochemistry · 1990
• PMID 2169766 Biol. Chem. Hoppe-Seyler · 1990
• Partial amino acid sequence of human PMN leukocyte procollagenase. Biol. Chem. Hoppe-Seyler · 1990
• Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases. J. Biol. Chem. · 1990
• Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms. Eur. J. Biochem. · 1990
• Mercurial activation of human polymorphonuclear leucocyte procollagenase. Eur. J. Biochem. · 1991
• … and 1 more in the literature graph