MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Crystal structure of the apoptotic suppressor CrmA in its cleaved form. Crystal structure of the apoptotic suppressor CrmA in its cleaved form. Structure (0969-2126) 2000 Renatus M., Zhou Q., Stennicke HR., Snipas SJ., Turk D., Bankston LA., Liddington RC., Salvesen GS. Virus - Publications including interactions involving viral proteins no in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Renatus M., Zhou Q., Stennicke HR., Snipas SJ., Turk D., Bankston LA., Liddington RC., Salvesen GS. Virus - Publications including interactions involving viral proteins no Structure (0969-2126) 2000 spi2_var67 Serine proteinase inhibitor 2 SPI-2 B13R B12R B14R protein protein varv Variola virus (isolate Human/India/Ind3/1967) VARV Smallpox virus MDIFREIASSTKGENVFISPATISSVLTILYYGANGSTAEQLSKYVEKEETMDKVSAQNISFKSMNKVYGRYSAVFKNSFLGKIGDNFQTVDFTDCRTIDAINKCVDVFTEGKINPLLTEQLSPNTCLLAISAVYFKAKWLIPFKKEFTSDYPFYVSPTEMVDVSMMSMYGESFNYASVKESFGNFSIIELPYVGNTSMMVILPDKIDGLESIKQNLTDTNFKKWCNSLEATFIDVHIPKFKVTGSYNLVDTLVKLGLTDVFYSTGDYSNMCNSDVSVDAMIHKTYIDVNEEYTEAAAATSVLVADCASTVTNEFCADHPFIYVIRHVDGKILFVGRYCSPTTN mint May be involved in the regulation of the complement cascade 4EAF2AEDD394D063 spi2_cwpxb Serine proteinase inhibitor 2 CRMA SPI-2 CPXV207 ICE inhibitor Cytokine response modifier protein A Hemorrhage-inducing 38 kDa protein protein protein cpv Cowpox virus (strain Brighton Red) MDIFREIASSMKGENVFISPPSISSVLTILYYGANGSTAEQLSKYVEKEADKNKDDISFKSMNKVYGRYSAVFKDSFLRKIGDNFQTVDFTDCRTVDAINKCVDIFTEGKINPLLDEPLSPDTCLLAISAVYFKAKWLMPFEKEFTSDYPFYVSPTEMVDVSMMSMYGEAFNHASVKESFGNFSIIELPYVGDTSMVVILPDNIDGLESIEQNLTDTNFKKWCDSMDAMFIDVHIPKFKVTGSYNLVDALVKLGLTEVFGSTGDYSNMCNSDVSVDAMIHKTYIDVNEEYTEAAAATCALVADCASTVTNEFCADHPFIYVIRHVDGKILFVGRYCSPTTN mint Specific and potent inhibitor of the interleukin-1-beta converting enzyme (ICE) thereby suppressing an interleukin-1 beta response to infection. The inhibition of ICE by crmA is an example of a "cross-class" interaction, in which a serpin inhibits a non-serine proteinase. Also inhibits granzyme B 25AE4E0CB123E172 crma-spi_2 1 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 2 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 direct interaction direct interaction In the xray complex 1f0c, P07385 is chain A and P33830 is chain B Resolution 2.260 homomint mint