Solution Structure of Monomeric Peptide YY Supports the Functional Significance of the PP-Fold†,‡

Biochemistry ◽  
2000 ◽  
Vol 39 (32) ◽  
pp. 9935-9942 ◽  
Author(s):  
David A. Keire ◽  
Mitsuo Kobayashi ◽  
Travis E. Solomon ◽  
Joseph R. Reeve
Keyword(s):  
Functional Significance ◽  
Solution Structure ◽  
Peptide Yy

Tumor Suppressor INK4:  Determination of the Solution Structure of p18INK4Cand Demonstration of the Functional Significance of Loops in p18INK4Cand p16INK4A †,‡

Biochemistry ◽  
1999 ◽  
Vol 38 (10) ◽  
pp. 2930-2940 ◽  
Author(s):  
Junan Li ◽  
In-Ja L. Byeon ◽  
Karen Ericson ◽  
Ming-Jye Poi ◽  
Paul O'Maille ◽  
...  
Keyword(s):  
Tumor Suppressor ◽  
Functional Significance ◽  
Solution Structure

Solution structure of γ-bungarotoxin: The functional significance of amino acid residues flanking the RGD motif in integrin binding

2004 ◽  
Vol 57 (4) ◽  
pp. 839-849 ◽  
Author(s):  
Jia-Hau Shiu ◽  
Chiu-Yueh Chen ◽  
Long-Sen Chang ◽  
Yi-Chun Chen ◽  
Yen-Chin Chen ◽  
...  
Keyword(s):  
Amino Acid ◽  
Functional Significance ◽  
Solution Structure ◽  
Amino Acid Residues ◽  
Rgd Motif

scholarly journals A structural comparison of the colicin immunity proteins Im7 and Im9 gives new insights into the molecular determinants of immunity-protein specificity

1998 ◽  
Vol 333 (1) ◽  
pp. 183-191 ◽  
Author(s):  
Caitríona A. DENNIS ◽  
Hortense VIDELER ◽  
Richard A. PAUPTIT ◽  
Russell WALLIS ◽  
Richard JAMES ◽  
...  
Keyword(s):  
Functional Significance ◽  
Solution Structure ◽  
Analytical Ultracentrifugation ◽  
Detailed Comparison ◽  
Molecular Replacement ◽  
Immunity Protein ◽  
Protein Specificity ◽  
Structural Framework ◽  
Endonuclease Domain ◽  
Colicin E9

We report the first detailed comparison of two immunity proteins which, in conjunction with recent protein engineering data, begins to explain how these structurally similar proteins are able to bind and inhibit the endonuclease domain of colicin E9 (E9 DNase) with affinities that differ by 12 orders of magnitude. In the present work, we have determined the X-ray structure of the Escherichia coli colicin E7 immunity protein Im7 to 2.0 Å resolution by molecular replacement, using as a trial model the recently determined NMR solution structure of Im9. Whereas the two proteins adopt similar four-helix structures, subtle structural differences, in particular involving a conserved tyrosine residue critical for E9 DNase binding, and the identity of key residues in the specificity helix, lie at the heart of their markedly different ability to bind the E9 DNase. Two other crystal structures were reported recently for Im7; in one, Im7 was a monomer and was very similar to the structure reported here, whereas in the other it was a dimer to which functional significance was assigned. Since this previous work suggested that Im7 could exist either as a monomer or a dimer, we used analytical ultracentrifugation to investigate this question further. Under a variety of solution conditions, we found that Im7 only ever exists in solution as a monomer, even up to protein concentrations of 15 mg/ml, casting doubt on the functional significance of the crystallographically observed dimer. This work provides a structural framework with which we can understand immunity-protein specificity, and in addition we believe it to be the first successfully refined crystal structure solved by molecular replacement using an NMR trial model with less than 100% sequence identity.

Functional significance of preserved color patterns of mollusks from the Gosport Sand (Eocene) of Alabama

1988 ◽  
Vol 62 (01) ◽  
pp. 83-87 ◽  
Author(s):  
Patricia H. Kelley ◽  
Charles T. Swann
Keyword(s):  
Functional Morphology ◽  
Functional Significance ◽  
Intraspecific Variability ◽  
Color Pattern ◽  
Color Patterns ◽  
Historical Factors ◽  
Life Mode ◽  
Molluscan Fauna ◽  
Excellent Preservation ◽  
Architectural Constraints

The excellent preservation of the molluscan fauna from the Gosport Sand (Eocene) at Little Stave Creek, Alabama, has made it possible to describe the preserved color patterns of 15 species. In this study the functional significance of these color patterns is tested in the context of the current adaptationist controversy. The pigment of the color pattern is thought to be a result of metabolic waste disposal. Therefore, the presence of the pigment is functional, although the patterns formed by the pigment may or may not have been adaptive. In this investigation the criteria proposed by Seilacher (1972) for testing the functionality of color patterns were applied to the Gosport fauna and the results compared with life mode as interpreted from knowledge of extant relatives and functional morphology. Using Seilacher's criteria of little ontogenetic and intraspecific variability, the color patterns appear to have been functional. However, the functional morphology studies indicate an infaunal life mode which would preclude functional color patterns. Particular color patterns are instead interpreted to be the result of historical factors, such as multiple adaptive peaks or random fixation of alleles, or of architectural constraints including possibly pleiotropy or allometry. The low variability of color patterns, which was noted within species and genera, suggests that color patterns may also serve a useful taxonomic purpose.

Complex Vesicles, Microtubules, and Cytoplasmic Filaments in the Endothelial Cells of Normal Dog Aorta

1968 ◽  
Vol 26 ◽  
pp. 172-173
Author(s):  
C. N. Sun ◽  
J. J. Ghidoni
Keyword(s):  
Electron Microscopy ◽  
Endothelial Cells ◽  
Cross Sections ◽  
Functional Significance ◽  
Tubular Structures ◽  
Aldehyde Fixation ◽  
Cytoplasmic Filaments

Endothelial cells in longitudinal and cross sections of aortas from 3 randomly selected “normal” mongrel dogs were studied by electron microscopy. Segments of aorta were distended with cold cacodylate buffered 5% glutaraldehyde for 10 minutes prior to being cut into small, well oriented tissue blocks. After an additional 1-1/2 hour period in glutaraldehyde, the tissue blocks were well rinsed in buffer and post-fixed in OsO4. After dehydration they were embedded in a mixture of Maraglas, D.E.R. 732, and DDSA.Aldehyde fixation preserves the filamentous and tubular structures (300 Å and less) for adequate demonstration and study. The functional significance of filaments and microtubules has been recently discussed by Buckley and Porter; the precise roles of these cytoplasmic components remains problematic. Endothelial cells in canine aortas contained an abundance of both types of structures.

Solution structure of cytochrome b5 mutant (E44/48/56A/D60A) and its interaction with cytochrome c

2001 ◽  
Vol 268 (6) ◽  
pp. 1620-1630
Author(s):  
Yibing Wu ◽  
Yunhua Wang ◽  
Chengmin Qian ◽  
Jun Lu ◽  
Ercheng Li ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Solution Structure ◽  
Cytochrome B5

Effect of circulating peptide YY on gallbladder motility in response to feeding in humans

2001 ◽  
Vol 120 (5) ◽  
pp. A14-A14 ◽  
Author(s):  
F HOENTJEN ◽  
W HOPMAN ◽  
J JANSEN
Keyword(s):  
Peptide Yy ◽  
Gallbladder Motility

Abnormal levels of neuropeptide Y and peptide YY in colon in the irritable bowel syndrome (IBS)

2001 ◽  
Vol 120 (5) ◽  
pp. A753-A754
Author(s):  
M SIMREN ◽  
G RINGSTROM ◽  
P STOTZER ◽  
H ABRAHAMSSON ◽  
E BJOMSSON
Keyword(s):  
Irritable Bowel Syndrome ◽  
Neuropeptide Y ◽  
Peptide Yy ◽  
Irritable Bowel
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