Neutrophil collagenase

Details

Name
Neutrophil collagenase
Synonyms
  • 3.4.24.34
  • CLG1
  • Matrix metalloproteinase-8
  • MMP-8
  • PMNL collagenase
  • PMNL-CL
Gene Name
MMP8
Organism
Humans
Amino acid sequence
>lcl|BSEQ0010824|Neutrophil collagenase
MFSLKTLPFLLLLHVQISKAFPVSSKEKNTKTVQDYLEKFYQLPSNQYQSTRKNGTNVIV
EKLKEMQRFFGLNVTGKPNEETLDMMKKPRCGVPDSGGFMLTPGNPKWERTNLTYRIRNY
TPQLSEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYQRDHGDNSPFDGPNGIL
AHAFQPGQGIGGDAHFDAEETWTNTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYA
FRETSNYSLPQDDIDGIQAIYGLSSNPIQPTGPSTPKPCDPSLTFDAITTLRGEILFFKD
RYFWRRHPQLQRVEMNFISLFWPSLPTGIQAAYEDFDRDLIFLFKGNQYWALSGYDILQG
YPKDISNYGFPSSVQAIDAAVFYRSKTYFFVNDQFWRYDNQRQFMEPGYPKSISGAFPGI
ESKVDAVFQQEHFFHVFSGPRYYAFDLIAQRVTRVARGNKWLNCRYG
Number of residues
467
Molecular Weight
53411.72
Theoretical pI
6.86
GO Classification
Functions
calcium ion binding / metalloendopeptidase activity / serine-type endopeptidase activity / zinc ion binding
Processes
collagen catabolic process / endodermal cell differentiation / extracellular matrix disassembly / extracellular matrix organization / proteolysis
Components
extracellular region / extracellular space / proteinaceous extracellular matrix
General Function
Zinc ion binding
Specific Function
Can degrade fibrillar type I, II, and III collagens.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic granule
Gene sequence
>lcl|BSEQ0010825|Neutrophil collagenase (MMP8)
ATGCAACAAATACCTCAAGAGAAGTCAATTAATGACTACCTGGAAAAGTTCTACCAATTA
CCAAGCAACCAGTATCAGTCTACAAGGAAGAATGGCACTAATGTGATCGTTGAAAAGCTT
AAAGAAATGCAGCGATTTTTTGGGTTGAATGTGACGGGGAAGCCAAATGAGGAAACTCTG
GACATGATGAAAAAGCCTCGCTGTGGAGTGCCTGACAGTGGTGGTTTTATGTTAACCCCA
GGAAACCCCAAGTGGGAACGCACTAACTTGACCTACAGGATTCGAAACTATACCCCACAG
CTGTCAGAGGCTGAGGTAGAAAGAGCTATCAAGGATGCCTTTGAACTCTGGAGTGTTGCA
TCACCTCTCATCTTCACCAGGATCTCACAGGGAGAGGCAGATATCAACATTGCTTTTTAC
CAAAGAGATCACGGTGACAATTCTCCATTTGATGGACCCAATGGAATCCTTGCTCATGCC
TTTCAGCCAGGCCAAGGTATTGGAGGAGATGCTCATTTTGATGCCGAAGAAACATGGACC
AACACCTCCGCAAATTACAACTTGTTTCTTGTTGCTGCTCATGAATTTGGCCATTCTTTG
GGGCTCGCTCACTCCTCTGACCCTGGTGCCTTGATGTATCCCAACTATGCTTTCAGGGAA
ACCAGCAACTACTCACTCCCTCAAGATGACATCGATGGCATTCAGGCCATCTATGGACTT
TCAAGCAACCCTATCCAACCTACTGGACCAAGCACACCCAAACCCTGTGACCCCAGTTTG
ACATTTGATGCTATCACCACACTCCGTGGAGAAATACTTTTCTTTAAAGACAGGTACTTC
TGGAGAAGGCATCCTCAGCTACAAAGAGTCGAAATGAATTTTATTTCTCTATTCTGGCCA
TCCCTTCCAACTGGTATACAGGCTGCTTATGAAGATTTTGACAGAGACCTCATTTTCCTA
TTTAAAGGCAACCAATACTGGGCTCTGAGTGGCTATGATATTCTGCAAGGTTATCCCAAG
GATATATCAAACTATGGCTTCCCCAGCAGCGTCCAAGCAATTGACGCAGCTGTTTTCTAC
AGAAGTAAAACATACTTCTTTGTAAATGACCAATTCTGGAGATATGATAACCAAAGACAA
TTCATGGAGCCAGGTTATCCCAAAAGCATATCAGGTGCCTTTCCAGGAATAGAGAGTAAA
GTTGATGCAGTTTTCCAGCAAGAACATTTCTTCCATGTCTTCAGTGGACCAAGATATTAC
GCATTTGATCTTATTGCTCAGAGAGTTACCAGAGTTGCAAGAGGCAATAAATGGCTTAAC
TGTAGATATGGCTGA
Chromosome Location
11
Locus
11q22.3
External Identifiers
ResourceLink
UniProtKB IDP22894
UniProtKB Entry NameMMP8_HUMAN
GenBank Protein ID180618
GenBank Gene IDJ05556
GenAtlas IDMMP8
HGNC IDHGNC:7175
General References
  1. Hasty KA, Pourmotabbed TF, Goldberg GI, Thompson JP, Spinella DG, Stevens RM, Mainardi CL: Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases. J Biol Chem. 1990 Jul 15;265(20):11421-4. [PubMed:2164002]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334]
  3. Knauper V, Kramer S, Reinke H, Tschesche H: 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 Apr 30;189(2):295-300. [PubMed:2159879]
  4. Blaser J, Knauper V, Osthues A, Reinke H, Tschesche H: Mercurial activation of human polymorphonuclear leucocyte procollagenase. Eur J Biochem. 1991 Dec 18;202(3):1223-30. [PubMed:1662606]
  5. Mallya SK, Mookhtiar KA, Gao Y, Brew K, Dioszegi M, Birkedal-Hansen H, Van Wart HE: Characterization of 58-kilodalton human neutrophil collagenase: comparison with human fibroblast collagenase. Biochemistry. 1990 Nov 27;29(47):10628-34. [PubMed:2176876]
  6. Knauper V, Kramer S, Reinke H, Tschesche H: Partial amino acid sequence of human PMN leukocyte procollagenase. Biol Chem Hoppe Seyler. 1990 May;371 Suppl:295-304. [PubMed:2169256]
  7. Knauper V, Kramer S, Reinke H, Tschesche H: Partial amino-acid sequence of human PMN leukocyte procollagenase. Biol Chem Hoppe Seyler. 1990 Aug;371(8):733. [PubMed:2169766]
  8. Blaser J, Triebel S, Reinke H, Tschesche H: Formation of a covalent Hg-Cys-bond during mercurial activation of PMNL procollagenase gives evidence of a cysteine-switch mechanism. FEBS Lett. 1992 Nov 16;313(1):59-61. [PubMed:1330697]
  9. Bode W, Reinemer P, Huber R, Kleine T, Schnierer S, Tschesche H: 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 Mar 15;13(6):1263-9. [PubMed:8137810]
  10. Reinemer P, Grams F, Huber R, Kleine T, Schnierer S, Piper M, Tschesche H, Bode W: Structural implications for the role of the N terminus in the 'superactivation' of collagenases. A crystallographic study. FEBS Lett. 1994 Jan 31;338(2):227-33. [PubMed:8307185]
  11. Stams T, Spurlino JC, Smith DL, Wahl RC, Ho TF, Qoronfleh MW, Banks TM, Rubin B: Structure of human neutrophil collagenase reveals large S1' specificity pocket. Nat Struct Biol. 1994 Feb;1(2):119-23. [PubMed:7656015]
  12. Betz M, Huxley P, Davies SJ, Mushtaq Y, Pieper M, Tschesche H, Bode W, Gomis-Ruth FX: 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 Jul 1;247(1):356-63. [PubMed:9249047]
  13. Brandstetter H, Engh RA, Von Roedern EG, Moroder L, Huber R, Bode W, Grams F: Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data. Protein Sci. 1998 Jun;7(6):1303-9. [PubMed:9655333]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB023261-Hydroxyamine-2-Isobutylmalonic AcidexperimentalunknownDetails
DB029532-Thiomethyl-3-Phenylpropanoic AcidexperimentalunknownDetails
DB032072-(Biphenyl-4-Sulfonyl)-1,2,3,4-Tetrahydro-Isoquinoline-3-Carboxylic AcidexperimentalunknownDetails
DB036222-Hydroxy-5-[4-(2-Hydroxy-Ethyl)-Piperidin-1-Yl]-5-Phenyl-1h-Pyrimidine-4,6-DioneexperimentalunknownDetails
DB03636GlycinamidexperimentalunknownDetails
DB03880BatimastatexperimentalunknownDetails
DB00786MarimastatinvestigationalyesinhibitorDetails
DB06971N-{2-[(4'-CYANO-1,1'-BIPHENYL-4-YL)OXY]ETHYL}-N'-HYDROXY-N-METHYLUREAexperimentalunknownDetails
DB07397(5S)-5-(2-amino-2-oxoethyl)-4-oxo-N-[(3-oxo-3,4-dihydro-2H-1,4-benzoxazin-6-yl)methyl]-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidine-2-carboxamideexperimentalunknownDetails
DB07713(1S)-1-{[(4'-methoxy-1,1'-biphenyl-4-yl)sulfonyl]amino}-2-methylpropylphosphonic acidexperimentalunknownDetails
DB07772(1R)-1-{[(4'-methoxy-1,1'-biphenyl-4-yl)sulfonyl]amino}-2-methylpropylphosphonic acidexperimentalunknownDetails
DB079003-FORMYL-2-HYDROXY-5-METHYL-HEXANOIC ACID HYDROXYAMIDEexperimentalunknownDetails
DB08028BUT-3-ENYL-[5-(4-CHLORO-PHENYL)-3,6-DIHYDRO-[1,3,4]THIADIAZIN-2-YLIDENE]-AMINEexperimentalunknownDetails
DB08403METHYLAMINO-PHENYLALANYL-LEUCYL-HYDROXAMIC ACIDexperimentalunknownDetails
DB084763-AMINO-AZACYCLOTRIDECAN-2-ONEexperimentalunknownDetails