. Protein domain structure of snake venom metalloproteinases (SVMPs) and associated molecules. molecules. Every domain or subdomain is represented by a unique color. M, metalloproteinase; D, Every single domain or subdomain is represented by a unique colour. M, metalloproteinase; D, disintegrin disintegrin (or disintegrin-like) domain; C, cysteine-rich domain; CW, cysteine-rich “wrist” (or disintegrin-like) domain; C, cysteine-rich domain; CW , cysteine-rich “wrist” subdomain; Ch , subdomain; Ch, the cysteine-rich “hand” subdomain; snaclec, snake venom C-type lectin-like domain; the cysteine-richgrowth element (EGF)-like domain; T, thrombospondin type-1 (TSP)domain; E, epidermal E, epidermal “hand” subdomain; snaclec, snake venom C-type lectin-like motif; S, spacer growth issue (EGF)-like domain; T, thrombospondin type-1 (TSP) motif; S,of SVMPs and domain; X, domain variable among ADAMTSs. Representatives of each and every class spacer domain; X, domain variable among ADAMTSs. Representatives determined, are indicated and ADAM/ADAMTSs, ADAM/ADAMTSs, whose crystal structure have already been of each class of SVMPs in red letters. The Pwhose classes SVMPs are divided into subclasses (IIIa IId) based onletters.distinct post-translation are III crystal structure have been determined, are indicated in red their The P-III classes SVMPs modifications. Recently, it was based on the distinct post-translation modifications. will not divided into subclasses (IIIa IId) located thattheirD domain of ADAMTS household proteinasesRecently, it was have a disintegrin-like structure but adopt the Ch subdomain fold, not have represented as D. structure found that the D domain of ADAMTS family members proteinases doesand as a result, isa disintegrin-like The previously C subdomain fold, andADAMTSs is structurallyD. The previously cysteine-richGh but adopt the cysteine-rich domain of thus, is represented as subdivided in to the N-terminal domain h subdomain-fold domain (C of ADAMTSs is structurally A) and the C-terminal N-terminal). The ADAMTS family members commonly ) and subdivided into the domain (CB Gh subdomain-fold domain (CA possesses the N-terminal M, D, T, C, S domains whereas the C-terminal is variable amongst ADAMTSs the C-terminal domain (CB ). The ADAMTS household typically possesses the N-terminal M, D, T, C, S e.g., ADAMTS13 possess six repeats of TSP and two CUB (complement, uEGF, and bone domains whereas the C-terminal is variable among ADAMTSs e.g., ADAMTS13 possess six repeats of morphogenesis) domains that stick to the S domain. Reproduced from [14], copyright 2012, Elsevier. TSP and two CUB (complement, uEGF, and bone morphogenesis) domains that follow the S domain. Reproduced from [14], copyright 2012, Elsevier.Protein E6 Protein web Figure 1.IL-34, Mouse (HEK293, His) Protein domain structure of snake venom metalloproteinases (SVMPs) and relatedToxins 2017, 9, 392 Toxins 2017, 9,four of 18 4 ofClass I (P-I) SVMPs, possess a single catalytic metalloproteinase (MP) domain in their mature form Class I (P-I) SVMPs, have a single catalytic metalloproteinase (MP) domain in their mature [23,28sirtuininhibitor0].PMID:24455443 All SVMPs exhibit an extended zinc-binding consensus sequence HEXXHXXGXXH/D, type [23,28sirtuininhibitor0]. All SVMPs exhibit an extended zinc-binding consensus sequence HEXXHXXGXXH/D, which comprises 3 zinc-coordinating histidine side chains, and normally, a glutamate residue. which comprises three zinc-coordinating histidine side chains, and commonly, a glutamate residue. Moreover, these proteins also possess a strictly conserved methionine c.