Critical Amino Acid Residues for the Specific Binding of the Ti-Recognizing Recombinant Ferritin with Oxide Surfaces of Titanium and Silicon

Langmuir ◽  
2009 ◽  
Vol 25 (18) ◽  
pp. 10901-10906 ◽  
Author(s):  
Tomohiro Hayashi ◽  
Ken-Ichi Sano ◽  
Kiyotaka Shiba ◽  
Kenji Iwahori ◽  
Ichiro Yamashita ◽  
...  
Keyword(s):  
Amino Acid ◽  
Specific Binding ◽  
Oxide Surfaces ◽  
Amino Acid Residues ◽  
Critical Amino Acid

Identification of Critical Amino Acid Residues for Human iNOS Functional Activity

2008 ◽  
Vol 27 (5) ◽  
pp. 309-318 ◽  
Author(s):  
Saule Naureckiene ◽  
Sreekumar R. Kodangattil ◽  
Edward J. Kaftan ◽  
Philip G. Jones ◽  
Jeffrey D. Kennedy ◽  
...  
Keyword(s):  
Amino Acid ◽  
Functional Activity ◽  
Amino Acid Residues ◽  
Critical Amino Acid

A703 CRITICAL AMINO ACID RESIDUES FOR THE ALLOSTERIC ACTIONS OF ISOFLURANE AND ENFLURANE IN THE HUMAN GABA sub A RECEPTOR

1997 ◽  
Vol 87 (Supplement) ◽  
pp. 703A
Author(s):  
N.L. Harrison ◽  
&NA; Mihic ◽  
Q. Ye ◽  
V. Koltchine ◽  
S. Finn ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Critical Amino Acid

scholarly journals Critical Amino Acid Residues Determine the Binding Affinity and the Ca2+ Release Efficacy of Maurocalcine in Skeletal Muscle Cells

2003 ◽  
Vol 278 (39) ◽  
pp. 37822-37831 ◽  
Author(s):  
Eric Estève ◽  
Sophia Smida-Rezgui ◽  
Sandor Sarkozi ◽  
Csaba Szegedi ◽  
Imed Regaya ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Binding Affinity ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Amino Acid Residues ◽  
Critical Amino Acid

scholarly journals H-2Kd-restricted antigenic peptides share a simple binding motif.

1991 ◽  
Vol 174 (3) ◽  
pp. 603-612 ◽  
Author(s):  
P Romero ◽  
G Corradin ◽  
I F Luescher ◽  
J L Maryanski
Keyword(s):  
Amino Acid ◽  
Mhc Class I ◽  
Specific Binding ◽  
Structural Features ◽  
Class I ◽  
Binding Motif ◽  
Antigenic Peptides ◽  
Amino Acid Residues ◽  
Antigenic Activity ◽  
Mhc Class I Molecule

We have defined structural features that are apparently important for the binding of four different, unrelated antigenic epitopes to the same major histocompatibility complex (MHC) class I molecule, H-2Kd. The four epitopes are recognized in the form of synthetic peptides by cytotoxic T lymphocytes of the appropriate specificity. By analysis of the relative potency of truncated peptides, we demonstrated that for each of the four epitopes, optimal antigenic activity was present in a peptide of 9 or 10 amino acid residues. A comparison of the relative competitor activity of the different-length peptides in a functional competition assay, as well as in a direct binding assay based on photoaffinity labeling of the Kd molecule, indicated that the enhanced potency of the peptides upon reduction in length was most likely due to a higher affinity of the shorter peptides for the Kd molecule. A remarkably simple motif that appears to be important for the specific binding of Kd-restricted peptides was identified by the analysis of peptides containing amino acid substitutions or deletions. The motif consists of two elements, a Tyr in the second position relative to the NH2 terminus and a hydrophobic residue with a large aliphatic side chain (Leu, Ile, or Val) at the COOH-terminal end of the optimal 9- or 10-mer peptides. We demonstrated that a simple peptide analogue (AYP6L) that incorporates the motif can effectively and specifically interact with the Kd molecule. Moreover, all of the additional Kd-restricted epitopes defined thus far in the literature contain the motif, and it may thus be useful for the prediction of new epitopes recognized by T cells in the context of this MHC class I molecule.

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