Roland Renetseder's research while affiliated with University of Groningen and other places
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Publications (9)
Bovine pancreatic phospholipase A2 covalently inhibited by p-bromo-phenacyl-bromide was crystallized from 50% (v/v) 2-methyl-2,4-pentanediol. The space group was P3121 with cell dimensions a = b = 46.73 Å and c = 102.5 Å (1 Å = 0.1 nm). Diffraction data were collected by oscillation photography from one single crystal of dimensions 0.2 mm × 0.2 mm...
Data collection has always been a time-consuming operation in protein X-ray crystallography. This situation drastically changed with the introduction of two-dimensional area detectors. In this article the first successful refinement of a protein structure using data collected with an Enraf-Nonius Fast Area-Scanning TV-detector (FAST) diffractometer...
The refined high resolution crystal structure of the bovine phospholipase A2 was compared with its counterpart from the venom of Crotalus atrox, the western diamondbacked rattlesnake. The strong similarity in their backbone conformations forms the basis of a common numbering system for the amino acid sequence. The three common major helices and muc...
Inhibition of enzymes is usually brought about by reagents which attack essential functional groups in the active site or by blocking the entrance to the active site. If one for example reacts the essential His 48 in phospholipase A2 with an acylating reagent such as p-bromophenacyl-bromide all activity is lost. However the activity of phospholipas...
The previously published three-dimensional structure of porcine pancreatic prophospholipase A2 at 3 A resolution was found to be incompatible with the structures of bovine phospholipase A2 and bovine prophospholipase A2. This was unexpected because of the very homologous amino acid sequences of these enzymes. Therefore, the crystal structure of the...
The previously published three-dimensional structure of porcine pancreatic prophospholipase A2 at 3resolution was found to be incompatible with the structures of bovine phospholipase A2 and bovine prophospholipase A2. This was unexpected because of the very homologous amino acid sequences of these enzymes. Therefore, the crystal structure of the po...
Citations
... Supplementary Fig. 1A, B), presenting a potential role that Asn21 can play at the substrate binding channel of hGIIE. GIB, from both human [6] and porcine [20], also has Asn at this position. However, in GIB, no structural change was observed around Asn21 before or after the ligand binding and the conformation of Asn21 is same as that in the inhibitor bound hGIIE structure (Supplementary Fig. 1B-D). ...
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... S. violaceoruber sPLA 2 (Sv-sPLA 2 ) contains only five -helices and two disulfide bonds (Matoba et al., 2002). In contrast, porcine pancreatic sPLA 2 (pp-sPLA 2 ) contains five -helices, one antiparallel -sheet and seven disulfide bonds (Dijkstra et al., 1983). Therefore, the overall structures of Sv-sPLA 2 (group XIV) and pp-sPLA 2 (group I) are significantly different. ...
... One subunit is an enzymatically active basic protein with a molecular mass of about 13.8 kDa, and the other one is an inactive acidic protein with a molecular mass of about 13.6 kDa. In the acidic subunit, the histidine residue at position 48 (amino acid numbering according to Renetseder et al. [27]) in the active center is replaced by glutamine. HDP-1 and HDP-2 manifest anticoagulant and anti-platelet activity. ...
... one for each component of the alpha doublet, by obvious extension of (11.2). These equations occur in § §2.2.3-5 of Thomas (1982a) in an older style of notation, and are known to fit experimental data as adjudged by the performance of the data-reduction routines run at Cambridge and elsewhere (Renetseder, Dijkstra, Kalk, Verpoorte & Drenth, 1986). This final model is thus an extension of that given by Thomas [1982e, §2.2.5, pp. ...
... On the other hand, p-BPB, besides blocking the catalytic center of Asp49 PLA 2 s, may induce subtle conformational changes at distant sites. Such changes have been shown by crystallography in the bovine pancreatic PLA 2 (Renetseder et al., 1988) and the non-myotoxic, acidic PLA 2 BthA-I from Bothrops jararacussu venom (Magro et al., 2005), although not in the case of the acidic APLA 2 from Agkistrodon halys venom (Zhao et al., 1998). Moreover, conformational changes induced by p-BPB have also been demonstrated for two Lys49 myotoxins, PrTX-I from B. pirajai (Marchi-Salvador et al., 2009) and BthTX-I from B. jararacussu (Fernandes et al., 2010). ...
