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| <scene name='41/411401/Cv/6'>Pig elastase</scene> (cyan, green) complex with <scene name='41/411401/Cv/5'>chymotrypsin/elastase isoinhibitor</scene> (magenta, yellow) (PDB code [[1eai]]). ELA <scene name='41/411401/Cv/7'>catalytic triad is Ser-His-Asp</scene>. | | <scene name='41/411401/Cv/6'>Pig elastase</scene> (cyan, green) complex with <scene name='41/411401/Cv/5'>chymotrypsin/elastase isoinhibitor</scene> (magenta, yellow) (PDB code [[1eai]]). ELA <scene name='41/411401/Cv/7'>catalytic triad is Ser-His-Asp</scene>.<ref>PMID:7922044</ref> |
| </StructureSection> | | </StructureSection> |
| ==3D structures of elastase== | | ==3D structures of elastase== |
Revision as of 08:54, 12 January 2016
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Elastase (ELA) is a chymotrypsin-like serine protease which breaks down proteins. The ELAs are numbered according to their genes. Panceatic ELA cleaves proteins at the carboxyl-terminal side of small neutral amino acids. It cleaves Ala-Ala and Ala-Gly bonds. [1] For additional details see Serine Proteases.
Relevance
ELA2 (or PMN-ELA) is secreted by neutrophils during inflammation.
Disease
Pulmonary emphysema is caused by the destruction of elastic fibre by elastase. Mutations in ELA2 are linked to the genetic disorder cyclic hematopoeiesis. Neutrophil elastase is involved in the blistering in bullose pemphigoid.
Structural highlights
Pig elastase (cyan, green) complex with chymotrypsin/elastase isoinhibitor (magenta, yellow) (PDB code 1eai). ELA catalytic triad is Ser-His-Asp.[2]
- ↑ Dominici R, Franzini C. Fecal elastase-1 as a test for pancreatic function: a review. Clin Chem Lab Med. 2002 Apr;40(4):325-32. PMID:12059069 doi:https://dx.doi.org/10.1515/CCLM.2002.051
- ↑ Huang K, Strynadka NC, Bernard VD, Peanasky RJ, James MN. The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase. Structure. 1994 Jul 15;2(7):679-89. PMID:7922044
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3D structures of elastase
Updated on 12-January-2016
{"openlevels":0}
- MMP12 See Serine Proteases
- MMP16 See 1eai
- ELA1
- 3mty, 3mu0, 3mu1, 3mu4, 3mu5, 3mu8, 3mnb, 3mnc, 3mns, 3mnx, 3mo3, 3mo6, 3mo9, 3moc, 3e3t, 2v0b, 2g4t, 2g4u, 2de8, 2blo, 2blq, 2a7c, 2a7j, 1gvk, 1qnj, 1lvy, 3est, 1est, 2oqu, 3odd, 3odf, 2bdc – pELA1 – pig
- 3hgn – pELA1+peptidyl inhibitor – neutron
- 3hgp, 2cv3, 2bdb, 2bcd, 2h1u, 1mmj, 1h9l, 1nes, 4est, 5est, 8est, 7est, 6est - pELA1+peptidyl inhibitor
- 1fzz – pELA1+ONO-6818
- 1qr3, 1qgf, 1bru, 1hv7, 1btu – pELA1+cyclic inhibitor
- 1okx – pELA1 + scyptolin
- 1e34, 1e35, 1e36, 1e37, 1e38 – pELA1-gamma-lactam
- 1eai – pELA1+Ascaris inhibitor
- 2d26 – pELA1+α-1-antitrypsin
- 1fle – pELA1+elafin
- 1b0e, 1b0f – pELA1+MDL
- 2v35 – pELA1+JM54
- 2iot – pELA1+clavulanic acid
- 2de9 – pELA1+tris
- 1uvo, 1uvp, 1lka, 1lkb – pELA1+ions
- 1gwa – pELA1+I3
- 1uo6, 1c1m – pELA1+Xe
- 1l0z, 1l1g - pELA1+Xe+Br
- 2bb4, 2bd2, 2bd3, 2bd4, 2bd5, 2bd7, 2bd8, 2bd9, 1hax, 1hay, 1haz, 1hb0, 1qix – pELA1+beta-casomorphin-7
- 2bda – pELA1+N-acetyl-NPI
- 1mcv – pELA1+squash inhibitor
- 1bma – pELA1+aminimide
- 1elf, 1elg – pELA1+peptidyl hydroxylamine
- 1eld, 1ele, 1elb, 1ela, 1elc, 2est – pELA1+anilide inhibitor
- 1esa, 1esb – pELA1 intermediate
- 1eas, 1eat, 1eau – pELA1+pyridine inhibitor
- 1inc – pELA1+benzoxazinone
- 1jim, 9est, 8est – pELA1+coumarin derivative
- 2fo9, 2foa, 2fob, 2foc, 2fod, 2foe, 2fof, 2fog, 2foh – pELA1+solvent
- 4k89 – PaELA – Pseudomonas aeruginosa
- 3dbk – PaELA+phophoramidon
- 1u4g – PaELA+HPI
- 1ezm - PaELA
- 1elt – ELA - salmon
- ELA2
- 3q76 – hELA2
- 3q77 – hELA2+dihydropyrimidone inhibitor
- 2z7f – hELA2 peptidase domain +antileukoproteinase
- 2rg3 – hELA2+sulfonic inhibitor
- 1h1b, 1ppg, 1hne – hELA2+inhibitor
- 1ppf – hELA2+ovomucoid
- 1b0f – hELA2+MDL101146
- 4nzl – hELA2 + protein
- 4wvp – hELA2 + activity-based probe
References
