Journal Issue - Volume 7 Issue 2 (February 1998)
Thank you, Hans!
- Ralph A. Bradshaw, David S. Eisenberg, Mark A. Hermodson, Joseph J. Villafranca, Brian W. Matthews, Robert T. Sauer
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070201 (p 231-232)
Domain assignment for protein structures using a consensus approach: Characterization and analysis
- Susan Jones, Michael Stewart, Alex Michie, Mark B. Swindells, Chirstine Orengo, Janet M. Thornton
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070202 (p 233-242)
Abstract A consensus approach for the assignment of structural domains in proteins is presented. The approach combines a number of previously published algorithms, and takes advantage of the elevated accuracy obtained when assignments from the individual algorithms are in agreement. The consensus approach is tested on a data set of 55 protein chains, for which domain assignments from four automated methods were known, and for which...
Hirunorms are true hirudin mimetics. The crystal structure of human α‐thrombin‐hirunorm V complex
- Giuseppina De Simone, Angela Lombardi, Stefania Galdiero, Flavia Nastri, Rossella Della Morte, Norma Staiano, Carlo Pedone, Martino Bolognesi, Vincenzo Pavone
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070203 (p 243-253)
Abstract A novel class of synthetic, multisite‐directed thrombin inhibitors, known as hirunorms, has been described recently. These compounds were designed to mimic the binding mode of hirudin, and they have been proven to be very strong and selective thrombin inhibitors. Here we report the crystal structure of the complex formed by human α‐thrombin and hirunorm V, a 26‐residue polypeptide containing non‐natural amino acids,...
Alignment algorithm for homology modeling and threading
- Nickolai N. Alexandrov, Roland Luethy
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070204 (p 254-258)
Abstract A DNA/protein sequence comparison is a popular computational tool for molecular biologists. Finding a good alignment implies an evolutionary and/or functional relationship between proteins or genomic loci. Sequential similarity between two proteins indicates their structural resemblance, providing a practical approach for structural modeling, when structure of one of these proteins is known. The first step in the homology...
Determination and analysis of antigenic epitopes of prostate specific antigen (PSA) and human glandular kallikrein 2 (hK2) using synthetic peptides and computer modeling
- Timo Piironen, Bruno O. Villoutreix, Charlotte Becker, Hans Lilja, Kelly Hollingsworth, Mauno Vihinen, Dominique Bridon, Xiaoxing Qiu, John Rapp, Barry Dowell, Timo Lövgren, Kim Pettersson, Hans Lilja
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070205 (p 259-269)
Abstract Prostate specific antigen (PSA) and human glandular kallikrein 2 (hK2), produced essentially by the prostate gland, are 237‐amino acid monomeric proteins, with 79% identity in primary structure. Twenty‐five anti‐PSA monoclonal antibodies (Mabs) were studied for binding to a large array of synthetic linear peptides selected from computer models of PSA and hK2, as well as to biotinylated peptides covering the entire PSA...
An interaction‐based analysis of calcium‐induced conformational changes in Ca 2+ sensor proteins
- Melanie R. Nelson, Walter J. Chazin
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070206 (p 270-282)
Abstract Calcium sensor proteins translate transient increases in intracellular calcium levels into metabolic or mechanical responses, by undergoing dramatic conformational changes upon Ca2+ binding. A detailed analysis of the calcium binding‐induced conformational changes in the representative calcium sensors calmodulin (CaM) and troponin C was performed to obtain insights into the underlying molecular basis for their response to ...
Structures of adamalysin II with peptidic inhibitors. Implications for the design of tumor necrosis factor α convertase inhibitors
- F. Xavier Gomis‐Rüth, Edgar F. Meyer, Lawrence F. Kress, Vincenzo Politi
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070207 (p 283-292)
Abstract Crotalus adamanteus snake venom adamalysin II is the structural prototype of the adamalysin or ADAM family comprising proteolytic domains of snake venom metalloproteinases, multimodular mammalian reproductive tract proteins, and tumor necrosis factor α convertase, TACE, involved in the release of the inflammatory cytokine, TNFα. The structure of adamalysin II in noncovalent complex with two small‐molecule right‐hand side...
Substrate binding and conformational changes of Clostridium glutamicum diaminopimelate dehydrogenase revealed by hydrogen/deuterium exchange and electrospray mass spectrometry
- Fang Wang, Giovanna Scapin, John S. Blanchard, Ruth Hogue Angeletti
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070208 (p 293-299)
Abstract C. glutamicum meso‐diaminopimelate dehydrogenase is an enzyme of the L‐lysine biosynthetic pathway in bacteria. The binding of NADPH and diaminopimelate to the recombinant, overexpressed enzyme has been analyzed using hydrogen/deuterium exchange and electrospray ionization/mass spectrometry. NADPH binding reduces the extent of deuterium exchange, as does the binding of diaminopimelate. Pepsin digestion of the deuterated...
Active‐site mobility in human immunodeficiency virus, type 1, protease as demonstrated by crystal structure of A28S mutant
- Lin Hong, Jean A. Hartsuck, Steve Foundling, Jacques Ermoliefe, Jordan Tang
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070209 (p 300-305)
Abstract The mutation Ala28 to serine in human immunodeficiency virus, type 1, (HIV‐1) protease introduces putative hydrogen bonds to each active‐site carboxyl group. These hydrogen bonds are ubiquitous in pepsin‐like eukaryotic aspartic proteases. In order to understand the significance of this difference between HIV‐1 protease and homologous, eukaryotic aspartic proteases, we solved the three‐dimensional structure of A28S mutant...
Apparent local stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: Implications for redox potential regulation and flavodoxin folding
- Elles Steensma, Melanie J. M. Nijman, Yves J. M. Bollen, P. Adrie De Jager, Willy A. M. Van Den Berg, Walter M.A. M. Van Dongen, Carlo P. M. Van Mierlo
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070210 (p 306-317)
Abstract As a first step to determine the folding pathway of a protein with an α/β doubly wound topology, the 1H, 13C, and 15N backbone chemical shifts of Azotobacter vinelandii holoflavodoxin II (179 residues) have been determined using multidimensional NMR spectroscopy. Its secondary structure is shown to contain a five‐stranded parallel β‐sheet (β2‐βl‐β3‐β4‐β5) and five α‐helices. Exchange rates for the individual amide protons of...
Identification of a specific tyrosine residue in Bryodin 1 distinct from the active site but required for full catalytic and cytotoxic activity
- Daniel K. Fryxell, Susan L. Gawlak, Robert W. Dodge, Clay B. Siegall
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070211 (p 318-324)
Abstract Bryodin 1 (BD1) is a type I ribosome‐inactivating protein (RIP) with low inherent animal toxicity. It has been cloned recently and the recombinant protein (rBDl) has been produced and crystallized. To gain insight into the relationship of rBDl structure and function, we investigated the role of sequences in a region (residues 128‐156) that exhibits homology with membrane interactive sequences and is not part of the...
Exploring sequence constraints on an interhelical turn using in vivo selection for catalytic activity
- Gavin Macbeath, Peter Kast, Donald Hilvert
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070212 (p 325-335)
Abstract The role of interhelical turns in determining protein structure has been investigated previously in relatively simple four‐helix‐bundle proteins using combinatorial mutagenesis coupled with screening for functional variants. To assess the tolerance to sequence substitution of a short, interhelical turn in a larger, more complicated protein, we have exploited a more sensitive in vivo selection for catalytic activity....
Interhelical contacts are required for the helix bundle fold of apolipophorin III and its ability to interact with lipoproteins
- Jianjun Wang, Vasanthy Narayanaswami, Robert O. Ryan, Brian D. Sykes
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070213 (p 336-341)
Abstract Apolipophorin‐III (apoLp‐III) from the insect, Manduca sexta, is a 166‐residue exchangeable apolipoprotein that plays a critical role in the dynamics of plasma lipoprotein interconversions. Our previous work indicated that a 36‐residue C‐terminal peptide fragment, generated by cyanogen bromide digestion of apoLp‐III, was unable to bind to lipid surfaces (Narayanaswami V, Kay CM, Oikawa K, Ryan RO, 1994, Biochemistry 33:13312‐13320),...
Solid‐state NMR studies of the membrane‐bound closed state of the colicin E1 channel domain in lipid bilayers
- Yongae Kim, Kathleen Valentine, Stanley J. Opella, Sharon L. Schendel, William A. Cramer
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070214 (p 342-348)
Abstract The colicin El channel polypeptide was shown to be organized anisotropically in membranes by solid‐state NMR analysis of samples of uniformly 15N‐labeled protein in oriented planar phospholipid bilayers. The 190 residue C‐terminal colicin E1 channel domain is the largest polypeptide to have been characterized by 15N solid‐state NMR spectroscopy in oriented membrane bilayers. The 15N‐NMR spectra of the colicin E1 show that: (1) the...
Reactivities of the S2 and S3 subsite residues of thrombin with the native and heparin‐induced conformers of antithrombin
- Alireza R. Rezaie
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070215 (p 349-357)
Abstract A pentasaccharide (PS) fragment of heparin capable of activating antithrombin (AT) markedly accelerates the inhibition of factor Xa by AT, but has insignificant effect on inhibition of thrombin. For inhibition of thrombin, the bridging function of a longer polysaccharide chain is required to accelerate the reaction. To study the basis for the similar reactivity of thrombin with the native or heparin‐activated conformers of...




