scholarly journals Crystal Structure of the Human Centromere Protein B (CENP-B) Dimerization Domain at 1.65-Å Resolution

2003 ◽  
Vol 278 (51) ◽  
pp. 51454-51461 ◽  
Author(s):  
Maki S. Tawaramoto ◽  
Sam-Yong Park ◽  
Yoshinori Tanaka ◽  
Osamu Nureki ◽  
Hitoshi Kurumizaka ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Dimerization Domain ◽  
Human Centromere ◽  
Centromere Protein ◽  
Protein B

Mapping of the Human Centromere Protein B Gene (CENPB) to Chromosome 20p13 by Fluorescence in Situ Hybridization

Genomics ◽  
1994 ◽  
Vol 24 (1) ◽  
pp. 187-188 ◽  
Author(s):  
Naohiko Seki ◽  
Toshiyuki Saito ◽  
Katsumi Kitagawa ◽  
Hiroshi Masumoto ◽  
Tuneko Okazaki ◽  
...  
Keyword(s):  
In Situ Hybridization ◽  
Fluorescence In Situ Hybridization ◽  
Human Centromere ◽  
Centromere Protein ◽  
Chromosome 20P13 ◽  
Protein B

scholarly journals An Antigenic Determinant on Human Centromere Protein B (CENP-B) A vailable for Production of Human-Specific Anticentromere Antibodies in Mouse.

1992 ◽  
Vol 17 (2) ◽  
pp. 129-138 ◽  
Author(s):  
Kenji Sugimoto ◽  
Hideyuki Migita ◽  
Yoshimasa Hagishita ◽  
Hiroaki Yata ◽  
Michio Himeno
Keyword(s):  
Antigenic Determinant ◽  
Human Centromere ◽  
Centromere Protein ◽  
Anticentromere Antibodies ◽  
Human Specific ◽  
Protein B

scholarly journals Human Centromere Protein B Induces Translational Positioning of Nucleosomes on α-Satellite Sequences

2005 ◽  
Vol 280 (50) ◽  
pp. 41609-41618 ◽  
Author(s):  
Yoshinori Tanaka ◽  
Hiroaki Tachiwana ◽  
Kinya Yoda ◽  
Hiroshi Masumoto ◽  
Tsuneko Okazaki ◽  
...  
Keyword(s):  
Human Centromere ◽  
Satellite Sequences ◽  
Centromere Protein ◽  
Protein B

scholarly journals Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9

2017 ◽  
Vol 37 (3) ◽  
Author(s):  
Lifang Sun ◽  
Pu Chen ◽  
Yintao Su ◽  
Zhixiong Cai ◽  
Lingwei Ruan ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Sodium Dodecyl ◽  
Titration Calorimetry ◽  
Pseudomonas Sp ◽  
Sterol Carrier Protein ◽  
Dimerization Domain ◽  
Alkyl Chains ◽  
Hydrolysis Of

A novel alkylsulfatase from bacterium Pseudomonas sp. S9 (SdsAP) was identified as a thermostable alkylsulfatases (type III), which could hydrolyze the primary alkyl sulfate such as sodium dodecyl sulfate (SDS). Thus, it has a potential application of SDS biodegradation. The crystal structure of SdsAP has been solved to a resolution of 1.76 Å and reveals that SdsAP contains the characteristic metallo-β-lactamase-like fold domain, dimerization domain, and C-terminal sterol carrier protein type 2 (SCP-2)-like fold domain. Kinetic characterization of SdsAP to SDS by isothermal titration calorimetry (ITC) and enzymatic activity assays of constructed mutants demonstrate that Y246 and G263 are important residues for its preference for the hydrolysis of ‘primary alkyl’ chains, confirming that SdsAP is a primary alkylsulfatase.

scholarly journals Structure of the N-terminal dimerization domain of CEACAM7

2015 ◽  
Vol 71 (9) ◽  
pp. 1169-1175 ◽  
Author(s):  
Daniel A. Bonsor ◽  
Dorothy Beckett ◽  
Eric J. Sundberg
Keyword(s):  
Crystal Structure ◽  
Hydrogen Bond ◽  
Sequence Variation ◽  
Cellular Adhesion ◽  
Sedimentation Equilibrium ◽  
Colorectal Cancers ◽  
Dimerization Domain ◽  
Adhesion Protein ◽  
Dimerization Interface ◽  
Colon And Rectum

CEACAM7 is a human cellular adhesion protein that is expressed on the surface of colon and rectum epithelial cells and is downregulated in colorectal cancers. It achieves cell adhesion through dimerization of the N-terminal IgV domain. The crystal structure of the N-terminal dimerization domain of CEACAM has been determined at 1.47 Å resolution. The overall fold of CEACAM7 is similar to those of CEACAM1 and CEACAM5; however, there are differences, the most notable of which is an insertion that causes theC′′ strand to buckle, leading to the creation of a hydrogen bond in the dimerization interface. TheKdimerizationfor CEACAM7 determined by sedimentation equilibrium is tenfold tighter than that measured for CEACAM5. These findings suggest that the dimerization affinities of CEACAMs are modulatedviasequence variation in the dimerization surface.

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