1985
DOI: 10.1111/j.1432-1033.1985.tb08762.x
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The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3)

Abstract: OMSVP3 and Oh4TKY3 (third domains of silver pheasant and turkey ovomucoid inhibitor) are Kazal-type serine proteinase inhbitors. They have been isomorphously crystallized in the monoclinic space group C2 with cell dimensions of a = 4.429 nm, b = 2.115 nm, c = 4.405 nm, /3 = 107". The asymmetric unit contains one molecule corresponding to an extremely low volume per unit molecular mass of 0.0017 nm3/Da. Data collection was only possible for the OMSVP3 crystals. Orientation and position of the OMSVP3 molecules i… Show more

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Cited by 121 publications
(86 citation statements)
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“…The loops of the interlocking double/3o~/~ proteins have been considered important for their function. Several protease inhibitors [ovomucoid (Bode, Epp, Huber, Laskowski & Ardelt, 1985), subtilisin carlesberg (Bode, Papamokos & Muskil, 1987), subtilisin bpn (Takeuchi, Satow, Nakamura & Mitsui, 1991)] use surface loops to bind to the active site. The activation domain of procarboxypeptidase may also inhibit the catalytic domain by means of a surface loop (Coil, Guasch, Aviles & Huber, 1991).…”
Section: Discussionmentioning
confidence: 99%
“…The loops of the interlocking double/3o~/~ proteins have been considered important for their function. Several protease inhibitors [ovomucoid (Bode, Epp, Huber, Laskowski & Ardelt, 1985), subtilisin carlesberg (Bode, Papamokos & Muskil, 1987), subtilisin bpn (Takeuchi, Satow, Nakamura & Mitsui, 1991)] use surface loops to bind to the active site. The activation domain of procarboxypeptidase may also inhibit the catalytic domain by means of a surface loop (Coil, Guasch, Aviles & Huber, 1991).…”
Section: Discussionmentioning
confidence: 99%
“…References: IGDl (Skarzynski et al, 1987), IGOX (Lindqvist, 1989), IIlB (Finzel et al, 1984), IPCY (Guss & Freeman, 1983), ZAPR (Suguna et al, 1987), ZCAB (Kannan et al, 1984), 2CPP (Poulos et al, 1987). 20VO (Bode et al, 1985), 2PRK (Betzel et al, 1988), 3DFR (Bolin et al, 1982). 6LDH (Abad-Zapatero et al, 1987).…”
Section: Cluster 131mentioning
confidence: 99%
“…Full-length follistatin comprises an N-terminal Fs0 domain; three consecutive repeats Fs1, Fs2, and Fs3; and a C-terminal acidic tail. B, structure-based sequence alignment of the three follistatin repeats with the follistatin-like domain of BM-40, the Kazal domains of the double-domain protease inhibitor rhodniin (1tbr, chain R, first Kazal domain) (39), the pancreatic secretory trypsin inhibitor (1tgs, chain I) (40), and silver pheasant ovomucoid (2ovo, chain A) (41), as well as a fragment of the EGF-like domain of blood coagulation factor VIIa (1dan, chain L) (42). Residues forming the EGF-like subdomain and the core of the Kazal-like subdomain are enclosed in a box, cysteines are highlighted in white over a black background, the disulfide connectivity is depicted with black lines, and individual disulfide bonds are numbered, along with Fs1 residues.…”
Section: Fig 1 Follistatin and Its Homologsmentioning
confidence: 99%