Solution structure of γ-bungarotoxin: The functional significance of amino acid residues flanking the RGD motif in integrin binding

2004 ◽  
Vol 57 (4) ◽  
pp. 839-849 ◽  
Author(s):  
Jia-Hau Shiu ◽  
Chiu-Yueh Chen ◽  
Long-Sen Chang ◽  
Yi-Chun Chen ◽  
Yen-Chin Chen ◽  
...  
Keyword(s):  
Amino Acid ◽  
Functional Significance ◽  
Solution Structure ◽  
Amino Acid Residues ◽  
Rgd Motif

scholarly journals Analysis of the functional significance of amino acid residues in the putative NTP-binding pattern of the poliovirus 2C protein

1992 ◽  
Vol 73 (8) ◽  
pp. 1977-1986 ◽  
Author(s):  
N. L. Teterina ◽  
K. M. Kean ◽  
A. E. Gorbalenya ◽  
V. I. Agol ◽  
M. Girard
Keyword(s):  
Amino Acid ◽  
Functional Significance ◽  
Binding Pattern ◽  
Amino Acid Residues

scholarly journals Solution structure and amino acid residues of C‐terminal RAGE (ctRAGE) involved in binding to Dia‐1 FH1 and its signaling

2011 ◽  
Vol 25 (S1) ◽  
Author(s):  
VIVEK RAI ◽  
Andres Maldonado ◽  
Shi‐Fang Yan ◽  
Ann Marie Schmidt ◽  
Alexander Shekhtman
Keyword(s):  
Amino Acid ◽  
Solution Structure ◽  
Amino Acid Residues

scholarly journals A Molecular Staple: D-Loops in the I Domain of Bacteriophage P22 Coat Protein Make Important Intercapsomer Contacts Required for Procapsid Assembly

2015 ◽  
Vol 89 (20) ◽  
pp. 10569-10579 ◽  
Author(s):  
Nadia G. D'Lima ◽  
Carolyn M. Teschke
Keyword(s):  
Amino Acid ◽  
Coat Protein ◽  
Solution Structure ◽  
Dna Packaging ◽  
Cross Linking ◽  
Coat Proteins ◽  
Fold Axis ◽  
Amino Acid Residues ◽  
Bacteriophage P22 ◽  
D Loop

ABSTRACTBacteriophage P22, a double-stranded DNA (dsDNA) virus, has a nonconserved 124-amino-acid accessory domain inserted into its coat protein, which has the canonical HK97 protein fold. This I domain is involved in virus capsid size determination and stability, as well as protein folding. The nuclear magnetic resonance (NMR) solution structure of the I domain revealed the presence of a D-loop, which was hypothesized to make important intersubunit contacts between coat proteins in adjacent capsomers. Here we show that amino acid substitutions of residues near the tip of the D-loop result in aberrant assembly products, including tubes and broken particles, highlighting the significance of the D-loops in proper procapsid assembly. Using disulfide cross-linking, we showed that the tips of the D-loops are positioned directly across from each other both in the procapsid and the mature virion, suggesting their importance in both states. Our results indicate that D-loop interactions act as “molecular staples” at the icosahedral 2-fold symmetry axis and significantly contribute to stabilizing the P22 capsid for DNA packaging.IMPORTANCEMany dsDNA viruses have morphogenic pathways utilizing an intermediate capsid, known as a procapsid. These procapsids are assembled from a coat protein having the HK97 fold in a reaction driven by scaffolding proteins or delta domains. Maturation of the capsid occurs during DNA packaging. Bacteriophage HK97 uniquely stabilizes its capsid during maturation by intercapsomer cross-linking, but most virus capsids are stabilized by alternate means. Here we show that the I domain that is inserted into the coat protein of bacteriophage P22 is important in the process of proper procapsid assembly. Specifically, the I domain allows for stabilizing interactions across the capsid 2-fold axis of symmetry via a D-loop. When amino acid residues at the tip of the D-loop are mutated, aberrant assembly products, including tubes, are formed instead of procapsids, consequently phage production is affected, indicating the importance of stabilizing interactions during the assembly and maturation reactions.

Functional significance of amino acid residues within conserved hydrophilic regions in human interferons-α

1989 ◽  
Vol 12 (1) ◽  
pp. 37-47 ◽  
Author(s):  
Martin J. Tymms ◽  
Beth McInnes ◽  
Gary J. Waine ◽  
Brian F. Cheetham ◽  
Anthony W. Linnane
Keyword(s):  
Amino Acid ◽  
Functional Significance ◽  
Amino Acid Residues

scholarly journals Thermal and Acidic Treatments of Gluten Epitopes Affect Their Recognition by HLA-DQ2 in silico

2021 ◽  
Vol 8 ◽  
Author(s):  
Jihui Gao ◽  
Haolan Du ◽  
Zekun Zhou ◽  
Zhongxin Liang ◽  
Hongrui Liang ◽  
...  
Keyword(s):  
Amino Acid ◽  
In Silico ◽  
Solution Structure ◽  
Wheat Gluten ◽  
Human Leukocyte ◽  
Dietary Exposure ◽  
Amino Acid Residues ◽  
Ph Change ◽  
Primary Amino ◽  
Hla Dq2

Celiac disease (CD) is a prevalent disorder with autoimmune features. Dietary exposure of wheat gluten (including gliadins and glutenins) to the small intestine activates the gluten-reactive CD4+ T cells and controls the disease development. While the human leukocyte antigen (HLA) is the single most important genetic factor of this polygenic disorder, HLA-DQ2 recognition of gluten is the major biological step among patients with CD. Gluten epitopes are often rich in Pro and share similar primary sequences. Here, we simulated the solution structures changes of a variety of gluten epitopes under different pH and temperatures, to mimic the fermentation and baking/cooking processes. Based on the crystal structure of HLA-DQ2, binding of differently processed gluten epitopes to DQ2 was studied in silico. This study revealed that heating and pH change during the fermentation process impact the solution structure of gluten epitope. However, binding of differently treated gluten epitope peptide (GEP) to HLA-DQ2 mainly depended on its primary amino acid sequence, especially acidic amino acid residues that play a pivotal role in their recognition by HLA-DQ2.

Functional significance of conserved amino acid residues

1992 ◽  
Vol 13 (1) ◽  
pp. 38-40 ◽  
Author(s):  
Anthony R. Poteete ◽  
Dale Rennell ◽  
Suzanne E. Bouvier
Keyword(s):  
Amino Acid ◽  
Functional Significance ◽  
Amino Acid Residues
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