Localization of the Cl-/HCO3-Anion Exchanger Binding Site to the Amino-Terminal Region of Carbonic Anhydrase II†

Biochemistry ◽  
2000 ◽  
Vol 39 (44) ◽  
pp. 13344-13349 ◽  
Author(s):  
John W. Vince ◽  
Uno Carlsson ◽  
Reinhart A. F. Reithmeier
Keyword(s):  
Carbonic Anhydrase ◽  
Binding Site ◽  
Anion Exchanger ◽  
Terminal Region ◽  
Carbonic Anhydrase Ii ◽  
Amino Terminal

Identification of the Carbonic Anhydrase II Binding Site in the Cl-/HCO3-Anion Exchanger AE1†

Biochemistry ◽  
2000 ◽  
Vol 39 (18) ◽  
pp. 5527-5533 ◽  
Author(s):  
John W. Vince ◽  
Reinhart A. F. Reithmeier
Keyword(s):  
Carbonic Anhydrase ◽  
Binding Site ◽  
Anion Exchanger ◽  
Carbonic Anhydrase Ii

Effect of the hydrogen bond network in carbonic anhydrase II zinc binding site. A theoretical study

1998 ◽  
Vol 76 (7) ◽  
pp. 1027-1032 ◽  
Author(s):  
Silvia Álvarez-Santos ◽  
Àngels González-Lafont ◽  
José M Lluch
Keyword(s):  
Hydrogen Bond ◽  
Carbonic Anhydrase ◽  
Binding Site ◽  
Zinc Binding ◽  
Carbonic Anhydrase Ii ◽  
Am1 Method ◽  
Hydrogen Bond Network ◽  
Zinc Binding Site ◽  
Bond Network ◽  
Metal Ligand

The hydrogen bond network influence on the carbonic anhydrase II (CAII) zinc binding site has been studied theoretically by using the semiempirical AM1 method. To this aim, quantum mechanical reduced models of wild-type CAII and several CAII variants have been constructed. We have shown that, when a direct metal ligand donates a hydrogen bond to an indirect metal ligand, the first-shell residues enhance their electrostatic interaction with the zinc cation. Thus, the hydrogen-bond network is able to modulate the zinc binding affinity and the zinc-water pKa.Key words: hydrogen bond network, carbonic anhydrase II, Zn2+ metalloenzyme ligands.

Engineering a cysteine ligand into the zinc binding site of human carbonic anhydrase II

Biochemistry ◽  
1993 ◽  
Vol 32 (38) ◽  
pp. 9896-9900 ◽  
Author(s):  
Laura L. Kiefer ◽  
Joseph F. Krebs ◽  
Steven A. Paterno ◽  
Carol A. Fierke
Keyword(s):  
Carbonic Anhydrase ◽  
Binding Site ◽  
Zinc Binding ◽  
Carbonic Anhydrase Ii ◽  
Zinc Binding Site ◽  
Human Carbonic Anhydrase

scholarly journals Importance of C-Terminal Knot Structure in Carbonic Anhydrase II (Part I): Role of C-Terminal Knot Forming GLN253 on Enzymatic Property of Human Carbinic II

1970 ◽  
Vol 14 ◽  
pp. 1-9
Author(s):  
Mohammad Taufiq Alam
Keyword(s):  
Amino Acid ◽  
Carbonic Anhydrase ◽  
Point Mutation ◽  
Amino Acid Residue ◽  
Active Site ◽  
Terminal Region ◽  
Carbonic Anhydrase Ii ◽  
C Terminus ◽  
Human Carbonic Anhydrase

In both, bovine and human carbonic anhydrase II, a conserved glutamine residue occupies the position in the middle of the knot, which is formed by intercrossing of C-terminal end with N-terminal region. Previous studies have indicated that C-terminus is not the part of an active site, but truncation of 7 amino acid residue in this region can have marked effects on stability of the enzyme (data not published). To gain further insight into the role of specific amino acid residue in C-terminal region, site directed mutagenesis was used to introduce point mutation. Substitution of glutamine with cysteine was chosen because the cysteine residue is less hydrophilic as compared with glutamine and thus, may disrupt the hydrophilic environment in this region. Result indicates that Gln253 located within the C-terminus knot topology plays a significant role in normal function of the enzyme. Thus, C-terminal region might mediate cooperativity between the central active site of the enzyme through proper formation of knot. Key words: Human carbonic anhydrase II; knot topology; point mutation J. bio-sci. 14: 1-9, 2006

scholarly journals Evidence for the location of the receptor-binding site of human erythropoietin at the carboxyl-terminal domain

Blood ◽  
1991 ◽  
Vol 77 (6) ◽  
pp. 1203-1210 ◽  
Author(s):  
MR Fibi ◽  
W Stuber ◽  
P Hintz-Obertreis ◽  
G Luben ◽  
D Krumwieh ◽  
...  
Keyword(s):  
Binding Site ◽  
Receptor Binding ◽  
Terminal Region ◽  
Biologically Active ◽  
Receptor Binding Site ◽  
Specific Antibodies ◽  
Amino Terminal ◽  
Human Erythropoietin ◽  
A Cell ◽  
Carboxyl Terminal

Abstract Five different peptides (P1: 84′95; P2: 152′166; P3: 52′63; P4: 7′23; P5: 110′123) homologous to relatively hydrophilic regions of human erythropoietin (huEpo) have been synthesized to identify biologically active domains of the hormone. All peptides were able to induce high titers of peptide-specific antibodies in rabbits. Antisera from rabbits induced by recombinant huEpo (rhuEpo) contained a relatively high amount of antibodies preferentially directed against three peptides (P2, P4, and P5), of which P4 comprised the amino-terminal region, P2 the carboxyl-terminus, and P5 an interior region previously described as the receptor-binding site. The same three peptides were able to induce rhuEpo-specific antibodies, whereas P1 and P3 lacked this activity. Only peptide-P2-induced antisera inhibited the biologic activity of rhuEpo in a cell proliferation assay, indicating that the carboxyl-terminal region of the molecule is essentially involved in the biologic function of rhuEpo.

A Novel Carbonic Anhydrase II Binding Site Regulates NHE1 Activity†

Biochemistry ◽  
2006 ◽  
Vol 45 (7) ◽  
pp. 2414-2424 ◽  
Author(s):  
Xiuju Li ◽  
Yongsheng Liu ◽  
Bernardo V. Alvarez ◽  
Joseph R. Casey ◽  
Larry Fliegel
Keyword(s):  
Carbonic Anhydrase ◽  
Binding Site ◽  
Carbonic Anhydrase Ii ◽  
Nhe1 Activity

scholarly journals Increased water flux induced by an aquaporin-1/carbonic anhydrase II interaction

2015 ◽  
Vol 26 (6) ◽  
pp. 1106-1118 ◽  
Author(s):  
Gonzalo Vilas ◽  
Devishree Krishnan ◽  
Sampath Kumar Loganathan ◽  
Darpan Malhotra ◽  
Lei Liu ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Mammalian Cells ◽  
Plasma Membranes ◽  
Close Association ◽  
Water Flux ◽  
Membrane Vesicles ◽  
Carbonic Anhydrase Ii ◽  
Physical Interaction ◽  
Aquaporin 1 ◽  
Amino Terminal

Aquaporin-1 (AQP1) enables greatly enhanced water flux across plasma membranes. The cytosolic carboxy terminus of AQP1 has two acidic motifs homologous to known carbonic anhydrase II (CAII) binding sequences. CAII colocalizes with AQP1 in the renal proximal tubule. Expression of AQP1 with CAII in Xenopus oocytes or mammalian cells increased water flux relative to AQP1 expression alone. This required the amino-terminal sequence of CAII, a region that binds other transport proteins. Expression of catalytically inactive CAII failed to increase water flux through AQP1. Proximity ligation assays revealed close association of CAII and AQP1, an effect requiring the second acidic cluster of AQP1. This motif was also necessary for CAII to increase AQP1-mediated water flux. Red blood cell ghosts resealed with CAII demonstrated increased osmotic water permeability compared with ghosts resealed with albumin. Water flux across renal cortical membrane vesicles, measured by stopped-flow light scattering, was reduced in CAII-deficient mice compared with wild-type mice. These data are consistent with CAII increasing water conductance through AQP1 by a physical interaction between the two proteins.

scholarly journals Eukaryotic Translation Initiation Factor 4E (eIF4E) Binding Site and the Middle One-Third of eIF4GI Constitute the Core Domain for Cap-Dependent Translation, and the C-Terminal One-Third Functions as a Modulatory Region

2000 ◽  
Vol 20 (2) ◽  
pp. 468-477 ◽  
Author(s):  
Shigenobu Morino ◽  
Hiroaki Imataka ◽  
Yuri V. Svitkin ◽  
Tatyana V. Pestova ◽  
Nahum Sonenberg
Keyword(s):  
Binding Site ◽  
Terminal Region ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Middle Region ◽  
Globin Mrna ◽  
Ribosome Binding ◽  
Amino Terminal ◽  
The Core ◽  
Core Sequence

ABSTRACT The mammalian eukaryotic initiation factor 4GI (eIF4GI) may be divided into three roughly equal regions; an amino-terminal one-third (amino acids [aa] 1 to 634), which contains the poly(A) binding protein (PABP) and eIF4E binding sites; a middle third (aa 635 to 1039), which binds eIF4A and eIF3; and a carboxy-terminal third (aa 1040 to 1560), which harbors a second eIF4A binding site and a docking sequence for the Ser/Thr kinase Mnk1. Previous reports demonstrated that the middle one-third of eIF4GI is sufficient for cap-independent translation. To delineate the eIF4GI core sequence required for cap-dependent translation, various truncated versions of eIF4GI were examined in an in vitro ribosome binding assay with β-globin mRNA. A sequence of 540 aa encompassing aa 550 to 1090, which contains the eIF4E binding site and the middle region of eIF4GI, is the minimal sequence required for cap-dependent translation. In agreement with this, a point mutation in eIF4GI which abolished eIF4A binding in the middle region completely inhibited ribosomal binding. However, the eIF4GI C-terminal third region, which does not have a counterpart in yeast, modulates the activity of the core sequence. When the eIF4A binding site in the C-terminal region of eIF4GI was mutated, ribosome binding was decreased three- to fourfold. These data indicate that the interaction of eIF4A with the middle region of eIF4GI is necessary for translation, whereas the interaction of eIF4A with the C-terminal region plays a modulatory role.

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