scholarly journals Inhibition of the Aminopeptidase fromAeromonas proteolyticaby Aliphatic Alcohols. Characterization of the Hydrophobic Substrate Recognition Site†

Biochemistry ◽  
1999 ◽  
Vol 38 (35) ◽  
pp. 11433-11439 ◽  
Author(s):  
Leila Ustynyuk ◽  
Brian Bennett ◽  
Tanya Edwards ◽  
Richard C. Holz
Keyword(s):  
Substrate Recognition ◽  
Aliphatic Alcohols ◽  
Recognition Site ◽  
Hydrophobic Substrate

The Role of Cytochrome 2B1 Substrate Recognition Site Residues 115, 294, 297, 298, and 362 in the Oxidation of Steroids and 7-Alkoxycoumarins

2001 ◽  
Vol 394 (1) ◽  
pp. 21-28 ◽  
Author(s):  
Tammy L. Domanski ◽  
You-Qun He ◽  
Emily E. Scott ◽  
Qinmi Wang ◽  
James R. Halpert
Keyword(s):  
Substrate Recognition ◽  
Recognition Site

Characterization of polyamines having agonist, antagonist, and inverse agonist effects at the polyamine recognition site of the NMDA receptor

Neuron ◽  
1990 ◽  
Vol 5 (2) ◽  
pp. 199-208 ◽  
Author(s):  
Keith Williams ◽  
Valina L. Dawson ◽  
Carmelo Romano ◽  
Marc A. Dichter ◽  
Perry B. Molinoff
Keyword(s):  
Nmda Receptor ◽  
Inverse Agonist ◽  
Recognition Site

scholarly journals Distinctive polymorphism at the HLA-C locus: implications for the expression of HLA-C.

1992 ◽  
Vol 176 (4) ◽  
pp. 937-950 ◽  
Author(s):  
J Zemmour ◽  
P Parham
Keyword(s):  
Polymerase Chain Reaction ◽  
T Cells ◽  
Cell Surface ◽  
Antigen Recognition ◽  
Recognition Site ◽  
Chain Reaction ◽  
Polymerase Chain ◽  
Selection For ◽  
Antigen Recognition Site

The HLA-C locus remains an enigma. The serological polymorphism is poorly defined, HLA-C molecules are expressed at the cell surface at about 10% the levels of HLA-A and -B, and their importance for antigen presentation to either CD8-bearing T cells or natural killer cells is unclear. Our understanding of HLA-C polymorphism has also lagged behind that of HLA-A and -B. We have applied the polymerase chain reaction to the characterization of cDNA encoding HLA-C antigens. Combining the recent results with previously characterized HLA-C alleles gives a data base of 26 sequences, which was used to analyze the nature of HLA-C polymorphism and compare it to the variation seen in HLA-A and -B. The sequences form 10 families of alleles that correlate well with the patterns of serological crossreactivity, including the C blanks, and all major HLA-C allelic families appear to have been sampled. The families further divide into two groups of HLA-C alleles defined on the basis of linked substitutions in the 3' exons. In comparison with HLA-A and -B, HLA-C alleles are more closely related to each other, there being less variation in residues of the antigen recognition site and more variation at other positions. In particular, the helix of the alpha 1 domain of HLA-C molecules is unusually conserved. Despite the reduced diversity in the antigen recognition site, it is evident that HLA-C genes have been the target of past selection for polymorphism. Within the antigen recognition site, it is the alpha 1 domain that is most diagnostic of HLA-C, whereas the alpha 2 domain is similar to that of HLA-B, the locus to which HLA-C is most closely related. In particular, conserved motifs in the alpha 1 helix and the conserved glycine at the base of the B pocket (position 45) provide a combination of features that is uniquely found in HLA-C molecules. We hypothesize that these features restrict the peptides bound by HLA-C molecules and in this manner reduce the efficiency of HLA-C assembly and expression at the cell surface. The overall picture HLA-C polymorphism obtained from this sampling of HLA-C alleles is unlikely to change as further alleles are characterized.

scholarly journals Structural Determinants of Aromatase Cytochrome P450 Inhibition in Substrate Recognition Site-1

2002 ◽  
Vol 16 (7) ◽  
pp. 1456-1468 ◽  
Author(s):  
Alan Conley ◽  
Samantha Mapes ◽  
C. Jo Corbin ◽  
Douglas Greger ◽  
Sandra Graham
Keyword(s):  
Cytochrome P450 ◽  
Substrate Recognition ◽  
Recognition Site ◽  
Structural Determinants
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