scholarly journals The CheZ Binding Interface of CheAS Is Located in α-Helix E

2009 ◽  
Vol 191 (18) ◽  
pp. 5845-5848 ◽  
Author(s):  
Christopher O'Connor ◽  
Philip Matsumura ◽  
Andres Campos
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Resonance Structure ◽  
Nuclear Magnetic Resonance Structure ◽  
Binding Interface ◽  
Α Helix ◽  
Interaction Surface ◽  
Nuclear Magnetic

ABSTRACT Specific CheA-short (CheAS) residues, L123 and L126, were identified as critical for CheZ binding. In the CheAS ′P1-CheZ nuclear magnetic resonance structure, these residues form an interaction surface on α-helix E in the ′P1 domain. Both L123 and L126 are buried in CheA-long (CheAL), providing an explanation for why CheAL fails to bind CheZ.

scholarly journals Novel β-Barrel Fold in the Nuclear Magnetic Resonance Structure of the Replicase Nonstructural Protein 1 from the Severe Acute Respiratory Syndrome Coronavirus

2007 ◽  
Vol 81 (7) ◽  
pp. 3151-3161 ◽  
Author(s):  
Marcius S. Almeida ◽  
Margaret A. Johnson ◽  
Torsten Herrmann ◽  
Michael Geralt ◽  
Kurt Wüthrich
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Severe Acute Respiratory Syndrome ◽  
Nonstructural Protein ◽  
Resonance Structure ◽  
Nuclear Magnetic Resonance Structure ◽  
Nonstructural Protein 1 ◽  
Viral Replicase ◽  
Α Helix ◽  
Nuclear Magnetic

ABSTRACT The nonstructural protein 1 (nsp1) of the severe acute respiratory syndrome coronavirus has 179 residues and is the N-terminal cleavage product of the viral replicase polyprotein that mediates RNA replication and processing. The specific function of nsp1 is not known. Here we report the nuclear magnetic resonance structure of the nsp1 segment from residue 13 to 128, which represents a novel α/β-fold formed by a mixed parallel/antiparallel six-stranded β-barrel, an α-helix covering one opening of the barrel, and a 310-helix alongside the barrel. We further characterized the full-length 179-residue protein and show that the polypeptide segments of residues 1 to 12 and 129 to 179 are flexibly disordered. The structure is analyzed in a search for possible correlations with the recently reported activity of nsp1 in the degradation of mRNA.

Nuclear Magnetic Resonance Structure of a Prototype Lin12-Notch Repeat Module from Human Notch1†

Biochemistry ◽  
2003 ◽  
Vol 42 (23) ◽  
pp. 7061-7067 ◽  
Author(s):  
Didem Vardar ◽  
Christopher L. North ◽  
Cheryll Sanchez-Irizarry ◽  
Jon C. Aster ◽  
Stephen C. Blacklow
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Resonance Structure ◽  
Nuclear Magnetic Resonance Structure ◽  
Nuclear Magnetic

scholarly journals Nuclear Magnetic Resonance Structure and IgE Epitopes of Blo t 5, a Major Dust Mite Allergen

2008 ◽  
Vol 181 (4) ◽  
pp. 2586-2596 ◽  
Author(s):  
Siew Leong Chan ◽  
Tan Ching Ong ◽  
Yun Feng Gao ◽  
Yuen Sung Tiong ◽  
De Yun Wang ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Mite Allergen ◽  
Resonance Structure ◽  
Nuclear Magnetic Resonance Structure ◽  
Dust Mite ◽  
Dust Mite Allergen ◽  
Nuclear Magnetic
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