scholarly journals Crystal structure and biochemical analyses reveal Beclin 1 as a novel membrane binding protein

Cell Research ◽  
2012 ◽  
Vol 22 (3) ◽  
pp. 473-489 ◽  
Author(s):  
Weijiao Huang ◽  
Wooyoung Choi ◽  
Wanqiu Hu ◽  
Na Mi ◽  
Qiang Guo ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Protein ◽  
Membrane Binding ◽  
Beclin 1 ◽  
Biochemical Analyses

Crystal Structure of the GTP-binding Protein Obg from Thermus thermophilus HB8

2004 ◽  
Vol 337 (3) ◽  
pp. 761-770 ◽  
Author(s):  
Mutsuko Kukimoto-Niino ◽  
Kazutaka Murayama ◽  
Mio Inoue ◽  
Takaho Terada ◽  
Jeremy R.H. Tame ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Protein ◽  
Thermus Thermophilus ◽  
Gtp Binding Protein ◽  
Thermus Thermophilus Hb8 ◽  
Gtp Binding

Detailed analysis of the atrial natriuretic factor receptor hormone-binding domain crystal structure

2001 ◽  
Vol 79 (8) ◽  
pp. 692-704 ◽  
Author(s):  
Focco van den Akker
Keyword(s):  
Crystal Structure ◽  
Atrial Natriuretic Factor ◽  
Binding Protein ◽  
Chloride Ion ◽  
Binding Domain ◽  
Protein Fold ◽  
Hormone Binding ◽  
Periplasmic Binding Protein ◽  
Natriuretic Factor ◽  
Hormone Binding Domain

The X-ray crystal structure of the dimerized atrial natriuretic factor (ANF) receptor hormone-binding domain has provided a first structural view of this anti-hypertensive receptor. The structure reveals a surprising evolutionary link to the periplasmic-binding protein fold family. Furthermore, the presence of a chloride ion in the membrane distal domain and the presence of a second putative effector pocket suggests that the extracellular domain of this receptor is allosterically regulated. The scope of this article is to extensively review the data published on this receptor and to correlate it with the hormone-binding domain structure. In addition, a more detailed description is provided of the important features of this structure including the different binding sites for the ANF hormone, chloride ion, putative effector pocket, glycosylation sites, and dimer interface.Key words: crystal structure, periplasmic-binding protein fold, guanylyl cyclase, hormone receptor.

Intact Ca(2+)-binding sites are required for targeting of annexin 1 to endosomal membranes in living HeLa cells

2000 ◽  
Vol 113 (22) ◽  
pp. 3931-3938 ◽  
Author(s):  
U. Rescher ◽  
N. Zobiack ◽  
V. Gerke
Keyword(s):  
Hela Cells ◽  
Binding Sites ◽  
Fluorescent Protein ◽  
Binding Protein ◽  
Membrane Binding ◽  
Growth Factor Receptor ◽  
Intracellular Distribution ◽  
Live Cells ◽  
Membrane Structures ◽  
Annexin 1

Annexin 1 is a Ca(2+)-regulated membrane binding protein and a major substrate of the epidermal growth factor receptor kinase. Because of its properties and intracellular distribution, the protein has been implicated in endocytic trafficking of the receptor, in particular in receptor sorting occurring in multivesicular endosomes. Up to now, however, the localization of annexin 1 to cellular membranes has been limited to subcellular fractionation and immunocytochemical analyses of fixed cells. To establish its localization in live cells, we followed the intracellular fate of annexin 1 molecules fused to the Green Fluorescent Protein (GFP). We show that annexin 1-GFP associates with distinct, transferrin receptor-positive membrane structures in living HeLa cells. A GFP chimera containing the Ca(2+)/phospholipid-binding protein core of annexin 1 also shows a punctate intracellular distribution, although the structures labeled here do not resemble early but, at least in part, late endosomes. In contrast, the cores of annexins 2 and 4 fused to GFP exhibit a cytoplasmic or a different punctate distribution, respectively, indicating that the highly homologous annexin core domains carry distinct membrane specificities within live cells. By inactivating the three high-affinity Ca(2+) binding sites in annexin 1 we also show that endosomal membrane binding of the protein in live HeLa cells depends on the integrity of these Ca(2+) binding sites. More detailed analysis identifies a single Ca(2+) site in the second annexin repeat that is crucially involved in establishing the membrane association. These results reveal for the first time that intracellular membrane binding of an annexin in living cells requires Ca(2+) and is mediated in part through an annexin core domain that is capable of establishing specific interactions.

scholarly journals Crystal structure of prokaryotic ribosomal protein L9: a bi-lobed RNA-binding protein.

1994 ◽  
Vol 13 (1) ◽  
pp. 205-212 ◽  
Author(s):  
D.W. Hoffman ◽  
C. Davies ◽  
S.E. Gerchman ◽  
J.H. Kycia ◽  
S.J. Porter ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ribosomal Protein ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Ribosomal Protein L9
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