scholarly journals Partial characterization of immunoglobulin Cµ gene of water buffalo (Bubalus bubalis) predicts distinct structural features of C1q-binding site in Cµ3 domain

2013 ◽  
pp. 19-23 ◽  
Author(s):  
Surinder S Saini ◽  
◽  
Maiti NK ◽  
Azad K Kaushik ◽  
◽  
...  
Keyword(s):  
Binding Site ◽  
Water Buffalo ◽  
Bubalus Bubalis ◽  
Structural Features ◽  
Partial Characterization

scholarly journals Partial Characterization of Immunoglobulin Cμ Gene of Water Buffalo (Bubalus bubalis) Predicts Distinct Structural Features of C1q-Binding Site in Cμ3 Domain

2013 ◽  
Vol 2013 ◽  
pp. 1-6
Author(s):  
Surinder S. Saini ◽  
N. K. Maiti ◽  
Azad K. Kaushik
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Water Buffalo ◽  
Helical Structure ◽  
Bubalus Bubalis ◽  
Structural Features ◽  
Partial Characterization ◽  
Protein Motif ◽  
High Amino Acid

Partial characterization of immunoglobulin Cµ gene of water buffalo (Bubalus bubalis) revealed high amino acid sequence identity with Cµ of cattle (94.28%) and sheep (91.71%). Four amino acid replacements (Met-301, Val-310, Asn-331, and Thr-432) in Cµ2, Cµ3, and Cµ4 of buffalo IgM are distinct, however. Unlike cattle, a codon deletion (GTG encoding valine at position 507 in cattle) and an insertion (GGC encoding glycine at position 532) occur in buffalo Cµ4. Three N-linked glycosylation (Asn-X-Thr/Ser) sites (one at position 325–327 in Cµ2; two at positions 372–374 and 394–396 in Cµ3) differentiate buffalo IgM from cattle and sheep. Similar to cattle, buffalo IgM has fewer prolines in Cµ2, which acts as hinge, which restricts Fab arm flexibility. Increased structural flexibility of the C1q-binding site in Cµ3 compensates for the rigid buffalo Cµ2 domain. Secondary structure of C1q-binding site is distinct in buffalo and cattle IgM where long alpha-helical structure is predominant that may be relevant to complement fixation function. Conserved protein motif “Thr-Cys-Thr-Val-Ala-His” provides protein signatures of C1q-binding region of ruminant species. The distinct structural features of C1q-binding site of buffalo and cattle IgM seem to be of functional significance and, therefore, useful in designing antibody based therapeutics.

scholarly journals Purification and partial characterization of a novel, non‐AT1, non‐AT2 binding site for angiotensins in the rat brain

2009 ◽  
Vol 23 (S1) ◽  
Author(s):  
Vardan T. Karamyan ◽  
Jason Arsenault ◽  
Klaus Klarskov ◽  
Zia Shariat‐Madar ◽  
Emanuel Escher ◽  
...  
Keyword(s):  
Binding Site ◽  
Rat Brain ◽  
Partial Characterization

scholarly journals Characterization of cathepsin S exosites that govern its elastolytic activity

2020 ◽  
Vol 477 (1) ◽  
pp. 227-242 ◽  
Author(s):  
Pierre-Marie Andrault ◽  
Preety Panwar ◽  
Dieter Brömme
Keyword(s):  
Binding Site ◽  
Structural Features ◽  
Docking Studies ◽  
Structural Examination ◽  
Structural Localization ◽  
Elastin Degradation ◽  
Basement Membrane Component ◽  
Elastolytic Activity ◽  
The Right

We have previously determined that the elastolytic activities of cathepsins (Cat) K and V require two exosites sharing the same structural localization on both enzymes. The structural features involved in the elastolytic activity of CatS have not yet been identified. We first mutated the analogous CatK and V putative exosites of CatS into the elastolytically inactive CatL counterparts. The modification of the exosite 1 did not affect the elastase activity of CatS whilst mutation of the Y118 of exosite 2 decreased the cleavage of elastin by ∼70% without affecting the degradation of other macromolecular substrates (gelatin, thyroglobulin). T06, an ectosteric inhibitor that disrupt the elastolytic activity of CatK, blocked ∼80% of the elastolytic activity of CatS without blocking the cleavage of gelatin and thyroglobulin. Docking studies showed that T06 preferentially interacts with a binding site located on the Right domain of the enzyme, outside of the active site. The structural examination of this binding site showed that the loop spanning the L174N175G176K177 residues of CatS is considerably different from that of CatL. Mutation of this loop into the CatL-like equivalent decreased elastin degradation by ∼70% and adding the Y118 mutation brought down the loss of elastolysis to ∼80%. In addition, the Y118 mutation selectively reduced the cleavage of the basement membrane component laminin by ∼50%. In summary, our data show that the degradation of elastin by CatS requires two exosites where one of them is distinct from those of CatK and V whilst the cleavage of laminin requires only one exosite.

Molecular Characterization of the Coding Region and 5’ UTR of HSP70 Gene in Indian Riverine Buffalo Breeds

2021 ◽  
Author(s):  
Ravinder Singh ◽  
Ankita Gurao ◽  
S.K. Mishra ◽  
S.K. Niranjan ◽  
Vikas Vohra ◽  
...  
Keyword(s):  
Water Buffalo ◽  
Thermal Adaptation ◽  
Role Playing ◽  
Bubalus Bubalis ◽  
Hsp70 Gene ◽  
Coding Region ◽  
Physiological Factors ◽  
Flanking Region ◽  
Entire Gene

Background: HSP70 (Heat Shock Protein 70), plays a crucial role in nascent protein folding; the added challenges due to physiological factors demand stringent role-playing of such chaperones for tropical livestock such as water buffalo (Bubalus bubalis). Therefore to evaluate the variations at nucleotide level in HSP70 that could potentially unravel the molecular basis of thermal adaptation in the riverine buffalo breeds of India, the current study was targeted to sequence the CDS (Coding Sequence) and UTR (Untranslated Region) of the gene in a panel of 16 Indian riverine buffalo breeds. Methods: Blood samples were collected and genomic DNA was isolated followed by PCR standardized for the amplification of different fragments of the HSP70 gene using different sets of primer pairs covering the entire coding region and 5’UTR. Multiple amplicons generated to cover the entire gene were sequenced. Sequences were further analyzed manually for the identification of heterozygous animals to detect the polymorphic nucleotide sites and variation between breeds documented. Result: The HSP70 results suggest, the highly conserved nature of gene in buffalo. The only non-synonymous polymorphic site was found in the Toda buffalo breed (g.SNPC greater than T at position 14), resulting in amino acid change 5M greater than T. A total of 7 polymorphic sites were found in the 5’UTR flanking region. Additionally, two insertion/deletions (INDEL) of 30 and 1 nucleotide length were found in the 5’UTR.

Characterization of Sarcocystis fusiformis based on sequencing and PCR-RFLP in water buffalo (Bubalus bubalis) in Iran

2011 ◽  
Vol 109 (6) ◽  
pp. 1563-1570 ◽  
Author(s):  
Ahmad Oryan ◽  
Hassan Sharifiyazdi ◽  
Monire Khordadmehr ◽  
Sara Larki
Keyword(s):  
Water Buffalo ◽  
Bubalus Bubalis ◽  
Pcr Rflp ◽  
Sarcocystis Fusiformis

Characterization of the extracellular matrix in the chorioallantoic membrane of water buffalo ( Bubalus bubalis ) in early gestation

2019 ◽  
Vol 54 (10) ◽  
pp. 1313-1321
Author(s):  
Jéssica Borghesi ◽  
Higor da Silva Ferreira ◽  
Phelipe Oliveira Favaron ◽  
Lara Carolina Mario ◽  
Adriana Raquel de Almeida da Anunciação ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Water Buffalo ◽  
Chorioallantoic Membrane ◽  
Bubalus Bubalis ◽  
Early Gestation
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