Crystallization, crystal structure analysis and molecular model of the third domain of Japanese quail ovomucoid, a Kazal type inhibitor

Weber, Ernst; Papamokos, Evangelos; Bode, Wolfram; Huber, Robert; Kato, Ikuo; Laskowski, M.

doi:10.1016/0022-2836(81)90263-1

Cited by 73 publications

(32 citation statements)

References 23 publications

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“…An obvious reason for the structural difference of the Nterminal segments up to Glu-10 is the involvement of Leu-1 to Asp-7 of OMJPQ3 in an intermolecular four-stranded /?channel formed with the N-terminal segments of neighbouring molecules [2]. The corresponding segment of OMSVP3, which has an identical sequence, is fully defined by electron density and runs close to the molecular surface of (Fig.…”

Section: Omsvp3 and Omjpq3mentioning

confidence: 99%

“…The corresponding value for the tetragonal OMJPQ3 crystals is 0.0028 nm3/Da [2]. As a consequence, the OMSVP3 molecule is engaged in many intermolecular contacts (1 57 interactions, including 14 hydrogen bonds, of distances below 0.4 nm) distributed over the whole surface.…”

Section: Omsvp3 and Omjpq3mentioning

confidence: 99%

“…The high-resolution crystal structures of three different representatives of the Kazal family have been determined and crystallographically refined : four independent molecules per asymmetric unit of the third domain of Japanese quail ovomucoid inhibitor (OMJPQ3) [2,31, the third domain of turkey ovomucoid inhibitor (OMTKY3) complexed with the Abbreviations. OMSVP3, third domain of silver pheasant ovomucoid inhibitor; Oh4TKY3, third domain of turkey ovomucoid inhibitor; OMJPQ3, third domain of Japanese quail ovomucoid inhibitor; PSTI, porcine pancreatic trypsin inhibitor; SGPB, Streptomyces griseus protease B; r.m.s., root-mean-square; IFo\, IF& observed and computed structure amplitudes.…”

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confidence: 99%

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The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3)

Bode

Epp

Huber

et al. 1985

European Journal of Biochemistry

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121

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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 in the monoclinic unit cells were determined using Patterson search methods and the known structure of the third domain of Japanese quail ovomucoid (OMJPQ3) [Papamokos, E., Weber, E., Bode, W., Huber, R., Empie, M. W., Kato, I. Ovomucoid inhibitors are major constitutents of avian egg white. Generally they consist of three tandem domains, each of which is a strong inhibitor of serine proteases and belongs to the family of Kazal inhibitors. The specificity of the ovomucoid inhibitors is mainly determined by the P1 residue. The nomenclature of Schechter and Berger [l] is used for the numbering of the substrate amino acid residues 'towards the NH2-terminal and the COOH-terminal directions from the scissile bond. The detailed specificity is also affected by single residue changes in positions other than P1. In an attempt to unravel the detailed algorithm for predicting inhibitory specificity from the amino acid sequence the Purdue group has sequenced a large number of avian ovomucoid domains and compared their inhibitory properties. It was found that only changes of residues in contact with the enzyme are important. Such exchanges may affect the packing of the inhibitory enzyme interface but they may also alter the mainchain conformation of the binding segment itself. Structural studies of related inhibitors are required to clarify this problem.The high-resolution crystal structures of three different representatives of the Kazal family have been determined and crystallographically refined : four independent molecules per asymmetric unit of the third domain of Japanese quail ovomucoid inhibitor (OMJPQ3) [2, 31, the third domain of turkey ovomucoid inhibitor (OMTKY3) complexed with the Abbreviations. OMSVP3, third domain of silver pheasant ovomucoid inhibitor; Oh4TKY3, third domain of turkey ovomucoid inhibitor; OMJPQ3, third domain of Japanese quail ovomucoid inhibitor; PSTI, porcine pancreatic trypsin inhibitor; SGPB, Streptomyces griseus protease B; r.m.s., root-mean-square; IFo\, IF& observed and computed structure amplitudes.Streptomyces griseus protease B [4,5], and the porcine pancreatic secretory trypsin inhibitor (PSTI) complexed with bovine trypsinogen [6]. The sequence of OMSVP3 differs at six positions from OMJPQ3. Three of these changes occur at P2(17), Pl(18) and Pl'(19) around the reactive site. The P3 to P2' residues run as follows: Cys-16, Thr-17, Met-18, Glu-19, Tyr-20. Thus, in contrast to OMJPQ3, which is a trypsin inhibitor because of a lysine residue at its PI position, the methionine of OMS...

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Section: Omsvp3 and Omjpq3mentioning

confidence: 99%

Section: Omsvp3 and Omjpq3mentioning

confidence: 99%

mentioning

confidence: 99%

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The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3)

Bode

Epp

Huber

et al. 1985

European Journal of Biochemistry

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121

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“…2). Due to a large deletion, however, the helix is one turn shorter than that in Japanese quail ovomucoid third domain (22) or either domain of rhodniin (24) (Fig. 2).…”

Section: Crystal Structure Of Ldti In Complex With Porcine Trypsin-mentioning

confidence: 99%

“…LDTI inhibits tryptase with a K i of 1.4 nM and, in addition, trypsin and chymotrypsin in the nanomolar range. Together with the plasmin inhibitor bdellin B-3 from H. medicinalis (20) and the thrombin inhibitor rhodniin from Rhodnius prolixus (21), LDTI belongs to a small group of nonclassical Kazal-type inhibitors related to, for example, the Japanese quail ovomucoid inhibitor (22) but exhibiting a distinctive disulfide pattern (Table I). We have recently solved the structure of rLDTI in solution (23) and that of rhodniin in complex with thrombin (24).…”

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The Three-dimensional Structure of Recombinant Leech-derived Tryptase Inhibitor in Complex with Trypsin

Stubbs

Morenweiser

Stürzebecher³

et al. 1997

Journal of Biological Chemistry

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The x-ray crystal structure of recombinant leech-derived tryptase inhibitor (rLDTI) has been solved to a resolution of 1.9 Å in complex with porcine trypsin. The nonclassical Kazal-type inhibitor exhibits the same overall architecture as that observed in solution and in rhodniin. The complex reveals structural aspects of the mast cell proteinase tryptase. The conformation of the binding region of rLDTI suggests that tryptase has a restricted active site cleft. The basic amino terminus of rLDTI, apparently flexible from previous NMR measurements, approaches the 148-loop of trypsin. This loop has an acidic equivalent in tryptase, suggesting that the basic amino terminus could make favorable electrostatic interactions with the tryptase molecule. A series of rLDTI variants constructed to probe this hypothesis confirmed that the amino-terminal Lys-Lys sequence plays a role in inhibition of human lung tryptase but not of trypsin or chymotrypsin. The location of such an acidic surface patch is in accordance with the known low molecular weight inhibitors of tryptase.

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Molecular Recognition in Biology: Models for Analysis of Protein—Ligand Interactions

Lancet

Horovitz

Katchalski‐Katzir

1994

Perspectives in Supramolecular Chemistry

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Crystallization, crystal structure analysis and molecular model of the third domain of Japanese quail ovomucoid, a Kazal type inhibitor

Cited by 73 publications

References 23 publications

The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3)

The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3)

The Three-dimensional Structure of Recombinant Leech-derived Tryptase Inhibitor in Complex with Trypsin

Molecular Recognition in Biology: Models for Analysis of Protein—Ligand Interactions

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