<scp>VAP</scp>1—Snake Venom Homolog of Mammalian<scp>ADAMs</scp>

Takeda, Soichi

doi:10.1002/0470028637.met234

Cited by 6 publications

(5 citation statements)

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“…Crystal structures of nine P-I SVMPs are currently available in the Protein Data Bank (PDB). Vascular apoptosis-inducing protein-1 (VAP1) [204,205], a P-IIIc dimeric class SVMP isolated from Crotalus atrox venom, is the first P-III SVMP structure to be solved [206,207]. To date, structures of seven P-III SVMPs have been deposited in the PDB and they include almost all P-III subclass structures.…”

Section: Related Mammalian Proteinsmentioning

confidence: 99%

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Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis

et al. 2011

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Snake venoms are cocktails of enzymes and non‐enzymatic proteins used for both the immobilization and digestion of prey. The most common snake venom enzymes include acetylcholinesterases, l‐amino acid oxidases, serine proteinases, metalloproteinases and phospholipases A2. Higher catalytic efficiency, thermal stability and resistance to proteolysis make these enzymes attractive models for biochemists, enzymologists and structural biologists. Here, we review the structures of these enzymes and describe their structure‐based mechanisms of catalysis and inhibition. Some of the enzymes exist as protein complexes in the venom. Thus we also discuss the functional role of non‐enzymatic subunits and the pharmacological effects of such protein complexes. The structures of inhibitor–enzyme complexes provide ideal platforms for the design of potent inhibitors which are useful in the development of prototypes and lead compounds with potential therapeutic applications.

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Section: Related Mammalian Proteinsmentioning

confidence: 99%

“…There are three disulfide bonds in the D s subdomain, three in D a and one in C w , and these subdomains are connected by a single disulfide bond. The residues coordinating the calcium ions and forming disulfide bonds are highly conserved among P-III SVMPs and ADAMs [206,207].…”

Section: Non-catalytic Domains Of P-iii Svmpsmentioning

confidence: 99%

Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis

et al. 2011

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“…The D-domain that follows the metalloproteinase domain (M-domain) is seen in VAP1 and VAP2B and divided into 2 sub-domains, the “D-shoulder” (Ds) and ‘‘D-arm” (Da) ( Figure 3 ). Both the Ds (residues 396–440) and Da subdomains (residues 441–487) contain calcium-binding sites [ 64 , 65 , 66 ]. ADAM-22 contains three putative calcium ions, two in the D-domain and one in the M-domain M, metalloproteinase-like domain (residues 233–435).…”

Section: Structural Model Of the Disintegrin-like Domains Of Adamsmentioning

confidence: 99%

“…The Ds- and Da subdomains consist of a series of turns and two short regions of antiparallel β-sheet forming a continuous C-shaped structure, which, along with the N-terminal region of the C-domain, forms a “C-wrist” (Cw) segment. The Cw segment is followed by a ‘‘C-hand” (Ch) segment with a hypervariable region (HVR) at its distal portion [ 65 ]. These structural features are summarized in the schematic shown in Figure 3 .…”

Section: Structural Model Of the Disintegrin-like Domains Of Adamsmentioning

confidence: 99%

ADAM-15 Disintegrin-Like Domain Structure and Function

Scully

Kakkar

et al. 2010

Toxins

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The ADAM (a disintegrin-like and metalloproteinase) proteins are a family of transmembrane cell-surface proteins with important functions in adhesion and proteolytic processing in all animals. Human ADAM-15 is the only member of the ADAM family with the integrin binding motif Arg-Gly-Asp (RGD) in its disintegrin-like domain. This motif is also found in most snake venom disintegrins and other disintegrin-like proteins. This unique RGD motif within ADAM-15 serves as an integrin ligand binding site, through which it plays a pivotal role in interacting with integrin receptors, a large family of heterodimeric transmembrane glycoproteins. This manuscript will present a review of the RGD-containing disintegrin-like domain structures and the structural features responsible for their activity as antagonists of integrin function in relation to the canonical RGD template.

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“…The M12B proteinases are also referred to as adamalysins or repropysins, nomenclatures chosen to reflect the two distinct origins of proteins in this class: the first family member to be structurally characterized was adamalysin II from rep tile venom, whereas others belong to a group of proteinases initially described in male repro ductive tissues [ 41 , 42 , 43 ]. Structure–function studies of the M12B proteinases were reviewed several years ago [ 44 , 45 , 46 , 47 ]. This review will update our knowledge of the three-dimensional structures of M12B proteinases and describe details of the structural features of their unique domains that may collaboratively participate in directing these proteinases to specific substrates.…”

Section: Introductionmentioning

confidence: 99%

ADAM and ADAMTS Family Proteins and Snake Venom Metalloproteinases: A Structural Overview

Takeda

2016

Toxins

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A disintegrin and metalloproteinase (ADAM) family proteins constitute a major class of membrane-anchored multidomain proteinases that are responsible for the shedding of cell-surface protein ectodomains, including the latent forms of growth factors, cytokines, receptors and other molecules. Snake venom metalloproteinases (SVMPs) are major components in most viper venoms. SVMPs are primarily responsible for hemorrhagic activity and may also interfere with the hemostatic system in envenomed animals. SVMPs are phylogenetically most closely related to ADAMs and, together with ADAMs and related ADAM with thrombospondin motifs (ADAMTS) family proteinases, constitute adamalysins/reprolysins or the M12B clan (MEROPS database) of metalloproteinases. Although the catalytic domain structure is topologically similar to that of other metalloproteinases such as matrix metalloproteinases, the M12B proteinases have a modular structure with multiple non-catalytic ancillary domains that are not found in other proteinases. Notably, crystallographic studies revealed that, in addition to the conserved metalloproteinase domain, M12B members share a hallmark cysteine-rich domain designated as the “ADAM_CR” domain. Despite their name, ADAMTSs lack disintegrin-like structures and instead comprise two ADAM_CR domains. This review highlights the current state of our knowledge on the three-dimensional structures of M12B proteinases, focusing on their unique domains that may collaboratively participate in directing these proteinases to specific substrates.

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VAP1—Snake Venom Homolog of MammalianADAMs

Cited by 6 publications

References 100 publications

Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis

Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis

ADAM-15 Disintegrin-Like Domain Structure and Function

ADAM and ADAMTS Family Proteins and Snake Venom Metalloproteinases: A Structural Overview

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