Notch ligand delta-like1: X-ray crystal structure and binding affinity

2015 ◽  
Vol 468 (1) ◽  
pp. 159-166 ◽  
Author(s):  
Nadia J. Kershaw ◽  
Nicole L. Church ◽  
Michael D.W. Griffin ◽  
Cindy S. Luo ◽  
Timothy E. Adams ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Affinity ◽  
Receptor Binding ◽  
Binding Sites ◽  
Notch Ligand ◽  
X Ray ◽  
Ligand Structure ◽  
Similarities And Differences

This X-ray crystal structure of the ectodomain of delta-like ligand-1 (Dll-1) represents the largest fragment of any Notch ligand structure to date. Comparison with the Jagged1 structures reveals similarities and differences between the ligand families and potential receptor binding sites.

scholarly journals Crystal Chemical Relations in the Shchurovskyite Family: Synthesis and Crystal Structures of K2Cu[Cu3O]2(PO4)4 and K2.35Cu0.825[Cu3O]2(PO4)4

Crystals ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 807
Author(s):  
Ilya V. Kornyakov ◽  
Sergey V. Krivovichev
Keyword(s):  
Crystal Structure ◽  
Crystal Structures ◽  
Structural Complexity ◽  
Crystal Chemical ◽  
X Ray Diffraction ◽  
Complexity Measures ◽  
X Ray ◽  
The Family ◽  
Similarities And Differences ◽  
Related Compounds

Single crystals of two novel shchurovskyite-related compounds, K2Cu[Cu3O]2(PO4)4 (1) and K2.35Cu0.825[Cu3O]2(PO4)4 (2), were synthesized by crystallization from gaseous phase and structurally characterized using single-crystal X-ray diffraction analysis. The crystal structures of both compounds are based upon similar Cu-based layers, formed by rods of the [O2Cu6] dimers of oxocentered (OCu4) tetrahedra. The topologies of the layers show both similarities and differences from the shchurovskyite-type layers. The layers are connected in different fashions via additional Cu atoms located in the interlayer, in contrast to shchurovskyite, where the layers are linked by Ca2+ cations. The structures of the shchurovskyite family are characterized using information-based structural complexity measures, which demonstrate that the crystal structure of 1 is the simplest one, whereas that of 2 is the most complex in the family.

ChemInform Abstract: X-Ray Crystal Structure of a Bisubstrate Inhibitor Bound to the Enzyme Catechol-O-methyltransferase: A Dramatic Effect of Inhibitor Preorganization on Binding Affinity.

ChemInform ◽  
2010 ◽  
Vol 33 (8) ◽  
pp. no-no
Author(s):  
Christian Lerner ◽  
Armin Ruf ◽  
Volker Gramlich ◽  
Birgit Masjost ◽  
Gerhard Zuercher ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Affinity ◽  
Dramatic Effect ◽  
X Ray

X-ray Crystal Structure of a Bisubstrate Inhibitor Bound to the Enzyme Catechol-O-methyltransferase: A Dramatic Effect of Inhibitor Preorganization on Binding Affinity

2001 ◽  
Vol 113 (21) ◽  
pp. 4164-4166 ◽  
Author(s):  
Christian Lerner ◽  
Armin Ruf ◽  
Volker Gramlich ◽  
Birgit Masjost ◽  
Gerhard Zürcher ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Affinity ◽  
Dramatic Effect ◽  
X Ray

Thyrotrophin receptors in normal and neoplastic (primary and metastatic) canine thyroid tissue

1992 ◽  
Vol 132 (3) ◽  
pp. 461-468 ◽  
Author(s):  
C. P. Verschueren ◽  
G. R. Rutteman ◽  
J. H. Vos ◽  
J. E. Van Dijk ◽  
T. W. A. de Bruin
Keyword(s):  
Thyroid Carcinoma ◽  
Binding Affinity ◽  
Receptor Binding ◽  
Binding Sites ◽  
Thyroid Tissue ◽  
Thyroid Neoplasms ◽  
Tsh Receptor ◽  
Normal Thyroid ◽  
Thyroid Carcinomas ◽  
Receptor Number

ABSTRACT Thyrotrophin (TSH) is the conditional growth factor of thyroid epithelial cells. Abnormalities in TSH-receptor binding such as a low receptor number or low binding affinity may be a marker of thyroid carcinoma or metastases, or may exhibit a relationship with the functional variability of such tissues. The dog was used as a model to characterize TSH-receptor binding in normal thyroid tissues, naturally occurring thyroid neoplasms and distant metastases. In normal dog thyroid tissues, specific 125I-labelled TSH binding ranged from 2·7 to 15·5%, and low cross-reactivity with bovine LH (0·023%) was observed. One class of TSH-binding sites was found in eight normal thyroid tissues and 22 thyroid carcinomas; two normal thyroid tissues and one tumour exhibited two classes of binding sites. The concentration of binding sites was lower in the five carcinomas with reduced pertechnetate uptake (0·09 pmol/mg protein) than in the five thyroid neoplasms with increased uptake (0·19 pmol/mg) (P= 0·055). Compared with the original carcinoma tissues, TSH binding revealed a reduced binding affinity in eight out of eleven metastases. Two metastases showed a complete absence of TSH binding, suggesting that they were not dependent on TSH for growth. We conclude that one class of TSH-binding site is predominant in normal dog thyroid tissues and dog thyroid carcinomas. TSH could therefore contribute, at least in theory, to further growth of primary dog thyroid carcinomas. Secondly, assays measuring TSH binding may not be able to discriminate between malignant and benign dog thyroid tumours. TSH receptor number or affinity may be related to the functional variability of thyroid neoplasms. The absence of TSH binding in some metastases demonstrated that this characteristic can be acquired during the natural history of a differentiated thyroid carcinoma. Journal of Endocrinology (1992) 132, 461–468

Redox-responsive molybdenum mononitrosyl complexes incorporating cyclic polyether cation binding sites and x-ray crystal structure of [Mo(NO){HB(3,5-Me2C3N2H)3}{OCH2(CH2OCH2)3CH2O}]

1992 ◽  
Vol 31 (2) ◽  
pp. 263-267 ◽  
Author(s):  
Najat J. AlObaidi ◽  
Sithy S. Salam ◽  
Paul D. Beer ◽  
Christopher D. Bush ◽  
Thomas A. Hamor ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Sites ◽  
Cation Binding ◽  
X Ray ◽  
Redox Responsive
Sign in / Sign up

Export Citation Format

Share Document