scholarly journals Crystal Structure of Aminopeptidase N (Proteobacteria Alanyl Aminopeptidase) fromEscherichia coliand Conformational Change of Methionine 260 Involved in Substrate Recognition

2006 ◽  
Vol 281 (44) ◽  
pp. 33664-33676 ◽  
Author(s):  
Kiyoshi Ito ◽  
Yoshitaka Nakajima ◽  
Yuko Onohara ◽  
Masahide Takeo ◽  
Kanako Nakashima ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Conformational Change ◽  
Substrate Recognition ◽  
Aminopeptidase N ◽  
Alanyl Aminopeptidase

scholarly journals Crystal structure of ribonuclease A.d(ApTpApApG) complex. Direct evidence for extended substrate recognition.

1994 ◽  
Vol 269 (34) ◽  
pp. 21526-21531 ◽  
Author(s):  
J.C. Fontecilla-Camps ◽  
R. de Llorens ◽  
M.H. le Du ◽  
C.M. Cuchillo
Keyword(s):  
Crystal Structure ◽  
Direct Evidence ◽  
Substrate Recognition

Crystal Structure of the Complex of the Variable Domain of Antibody D1.3 and Turkey Egg White Lysozyme: A Novel Conformational Change in Antibody CDR-L3 Selects for Antigen

1996 ◽  
Vol 257 (5) ◽  
pp. 889-894 ◽  
Author(s):  
Bradford C. Braden ◽  
Barry A. Fields ◽  
Xavier Ysern ◽  
Fernando A. Goldbaum ◽  
William Dall'Acqua ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Conformational Change ◽  
Egg White ◽  
Variable Domain ◽  
Egg White Lysozyme

scholarly journals Crystal structure of aminopeptidase N from human pathogen Neisseria meningitidis

2007 ◽  
Vol 70 (1) ◽  
pp. 273-279 ◽  
Author(s):  
B. Nocek ◽  
R. Mulligan ◽  
M. Bargassa ◽  
F. Collart ◽  
A. Joachimiak
Keyword(s):  
Crystal Structure ◽  
Neisseria Meningitidis ◽  
Aminopeptidase N ◽  
Human Pathogen

scholarly journals Crystal Structure of Dengue Virus Type 1 Envelope Protein in the Postfusion Conformation and Its Implications for Membrane Fusion

2009 ◽  
Vol 83 (9) ◽  
pp. 4338-4344 ◽  
Author(s):  
Vinod Nayak ◽  
Moshe Dessau ◽  
Kaury Kucera ◽  
Karen Anthony ◽  
Michel Ledizet ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Dengue Virus ◽  
Conformational Change ◽  
Virus Type ◽  
Envelope Protein ◽  
Lipid Membrane ◽  
Ph Sensor ◽  
Endosomal Membrane ◽  
Domain Iii

ABSTRACT Dengue virus relies on a conformational change in its envelope protein, E, to fuse the viral lipid membrane with the endosomal membrane and thereby deliver the viral genome into the cytosol. We have determined the crystal structure of a soluble fragment E (sE) of dengue virus type 1 (DEN-1). The protein is in the postfusion conformation even though it was not exposed to a lipid membrane or detergent. At the domain I-domain III interface, 4 polar residues form a tight cluster that is absent in other flaviviral postfusion structures. Two of these residues, His-282 and His-317, are conserved in flaviviruses and are part of the “pH sensor” that triggers the fusogenic conformational change in E, at the reduced pH of the endosome. In the fusion loop, Phe-108 adopts a distinct conformation, forming additional trimer contacts and filling the bowl-shaped concavity observed at the tip of the DEN-2 sE trimer.

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