Pulsed EPR studies of the type 2 copper binding site in the mercury derivative of laccase

Biochemistry ◽  
1992 ◽  
Vol 31 (27) ◽  
pp. 6265-6272 ◽  
Author(s):  
Jinfeng Lu ◽  
Christopher J. Bender ◽  
John McCracken ◽  
Jack Peisach ◽  
John C. Severns ◽  
...  
Keyword(s):  
Binding Site ◽  
Copper Binding ◽  
Pulsed Epr ◽  
Mercury Derivative

scholarly journals The crystal structure of poplar apoplastocyanin at 1.8-A resolution. The geometry of the copper-binding site is created by the polypeptide.

1984 ◽  
Vol 259 (5) ◽  
pp. 2822-2825 ◽  
Author(s):  
T P Garrett ◽  
D J Clingeleffer ◽  
J M Guss ◽  
S J Rogers ◽  
H C Freeman
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Copper Binding

Spectroscopic Characterization of Recombinant Cu,Zn Superoxide Dismutase fromPhotobacterium leiognathiExpressed inEscherichia coli:  Evidence for a Novel Catalytic Copper Binding Site

Biochemistry ◽  
1997 ◽  
Vol 36 (23) ◽  
pp. 7109-7113 ◽  
Author(s):  
Dolly Foti ◽  
Bruno Lo Curto ◽  
Giovanni Cuzzocrea ◽  
M. Elena Stroppolo ◽  
Francesca Polizio ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Binding Site ◽  
Spectroscopic Characterization ◽  
Copper Binding ◽  
Inescherichia Coli

XAFS study of the high-affinity copper-binding site of human PrP 91–231 and its low-resolution structure in solution 1 1Edited by I. A. Wilson

2001 ◽  
Vol 311 (3) ◽  
pp. 467-473 ◽  
Author(s):  
S.Samar Hasnain ◽  
Loretta M. Murphy ◽  
Richard W. Strange ◽  
J.Günter Grossmann ◽  
Anthony R. Clarke ◽  
...  
Keyword(s):  
Binding Site ◽  
Copper Binding ◽  
Low Resolution ◽  
High Affinity ◽  
Structure In Solution ◽  
Resolution Structure

β-Pro7Ang III is a novel highly selective angiotensin II type 2 receptor (AT2R) agonist, which acts as a vasodepressor agent via the AT2R in conscious spontaneously hypertensive rats

2015 ◽  
Vol 129 (6) ◽  
pp. 505-513 ◽  
Author(s):  
Mark Del Borgo ◽  
Yan Wang ◽  
Sanja Bosnyak ◽  
Morimer Khan ◽  
Pia Walters ◽  
...  
Keyword(s):  
Cardiovascular Disease ◽  
Angiotensin Ii ◽  
Protein Binding ◽  
Binding Site ◽  
Spontaneously Hypertensive Rats ◽  
Protective Effects ◽  
Ang Ii ◽  
Hypertensive Rats ◽  
Spontaneously Hypertensive

We have synthesized a highly selective compound that is able to target a protein-binding site [called angiotensin (Ang) II type 2 receptor, AT2R] in the cardiovascular system. This research tool will enhance our ability to stimulate AT2R to produce protective effects against cardiovascular disease.

scholarly journals High resolution structure of human apolipoprotein (a) kringle IV type 2: beyond the lysine binding site

2020 ◽  
Vol 61 (12) ◽  
pp. 1687-1696
Author(s):  
Alice Santonastaso ◽  
Maristella Maggi ◽  
Hugo De Jonge ◽  
Claudia Scotti
Keyword(s):  
High Resolution ◽  
Binding Site ◽  
Small Molecule ◽  
Aminocaproic Acid ◽  
Variable Number ◽  
Crystallographic Structure ◽  
Heparin Binding ◽  
Human Apolipoprotein ◽  
Unique Shape

Lipoprotein (a) [Lp(a)] is characterized by an LDL-like composition in terms of lipids and apoB100, and by one copy of a unique glycoprotein, apo(a). The apo(a) structure is mainly based on the repetition of tandem kringle domains with high homology to plasminogen kringles 4 and 5. Among them, kringle IV type 2 (KIV-2) is present in a highly variable number of genetically encoded repeats, whose length is inversely related to Lp(a) plasma concentration and cardiovascular risk. Despite it being the major component of apo(a), the actual function of KIV-2 is still unclear. Here, we describe the first high-resolution crystallographic structure of this domain. It shows a general fold very similar to other KIV domains with high and intermediate affinity for the lysine analog, ε-aminocaproic acid. Interestingly, KIV-2 presents a lysine binding site (LBS) with a unique shape and charge distribution. KIV-2 affinity for predicted small molecule binders was found to be negligible in surface plasmon resonance experiments; and with the LBS being nonfunctional, we propose to rename it “pseudo-LBS”. Further investigation of the protein by computational small-molecule docking allowed us to identify a possible heparin-binding site away from the LBS, which was confirmed by specific reverse charge mutations abolishing heparin binding. This study opens new possibilities to define the pathogenesis of Lp(a)-related diseases and to facilitate the design of specific therapeutic drugs.

An Artificial Metalloenzyme: Creation of a Designed Copper Binding Site in a Thermostable Protein

2010 ◽  
Vol 122 (30) ◽  
pp. 5277-5281 ◽  
Author(s):  
John Podtetenieff ◽  
Andreas Taglieber ◽  
Eckhard Bill ◽  
Edward J. Reijerse ◽  
Manfred T. Reetz
Keyword(s):  
Binding Site ◽  
Copper Binding ◽  
Thermostable Protein ◽  
Artificial Metalloenzyme
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