Table 1.
Selection of the 3D structures of the M12B proteinases deposited in the PDB.
| Protein | Source | Domains | PDB ID | Year | Reference | |
|---|---|---|---|---|---|---|
| ADAMs | ||||||
| ADAM8 | human | M | 4DD8 | 2012 | [68] | |
| ADAM10 | bovine | DC | 2AO7 | 2005 | [48] | |
| ADAM17 | human | M | 1BKC | 1998 | [64] | |
| ADAM17 | human | C | 2M2F (NMR) | 2013 | [69] | |
| ADAM22 | human | MDCE | 3G5C | 2009 | [65] | |
| ADAM33 | human | M | 1R54, 1R55 | 2004 | [70] | |
| ADAMTSs | ||||||
| ADAMTS1 | human | MD* | 2JIH, 2V4B | 2007 | [66] | |
| ADAMTS4 | human | MD* | 2RJP, 3B2Z | 2008 | [71] | |
| ADAMTS5 | human | M | 3B8Z | 2008 | [72] | |
| ADAMTS5 | human | MD* | 2RJQ | 2008 | [71] | |
| ADAMTS13 | human | D*TCS | 3GHM, 3GHN, 3VN4 | 2009 | [53,73] | |
| P-I SVMPs | ||||||
| acutolysin A | A. acutus | M | 1BSW, 1BUD | 1998 | [74] | |
| acutolysin C | A. acutus | M | 1QUA | 1999 | [75] | |
| adamalysin II | C. adamantus | M | 1IAG | 1993 | [42,76] | |
| atrolysin C | C. atrox | M | 1ATL, 1HTD | 1994 | [77] | |
| BaP1 | B. asper | M | 1ND1 | 2003 | [78] | |
| BmooMPα-I | B. moojeni | M | 3GBO | 2010 | [79] | |
| F II | A. acutus | M | 1YP1 | 2005 | [80] | |
| H2 proteinase | T. flavoviridis | M | 1WNI | 1996 | [81] | |
| TM-1 | T. mucrosquamatus | M | 4J4M | 2013 | [82] | |
| TM-3 | T. mucrosquamatus | M | 1KUF, 1KUG, 1KUI, 1KUK | 2002 | [83] | |
| P-IIIa/b SVMPs | ||||||
| AaHIV | A. acutus | MDC | 3HDB | 2009 | [84] | |
| atragin | N. atra | MDC | 3K7L | 2010 | [85] | |
| bothropasin | B. jararaca | MDC | 3DSL | 2008 | [86] | |
| catrocollastain/VAP2B | C. atrox | MDC | 2DW0, 2DQ1, 2DW2 | 2007 | [87] | |
| K-like | N. atra | MDC | 3K7N | 2010 | [85] | |
| P-IIIc SVMPs | ||||||
| VAP1 | C. atrox | 2x(MDC) | 2ERO, 2ERP, 2ERQ | 2006 | [28] | |
| P-IIId SVMPs | ||||||
| RVV-X | D. russelli | MDC+snaclec | 2E3X | 2007 | [88] | |
| multactivase | E. multisquamatus | DC+snaclec | unpublished | |||
* Despite its name, the D domain of ADAMTSs actually does not adopt a classic “disintegrin-like” tertiary structure, but has an ADAM_CR domain fold and is thus indicated as “D*”.