ZIB

Hits per page

hits 1 - 2 | 2 hits

Sorting

Electronic Resource

Molecular Modeling of the Domain Shared Between CED-4 and its Mammalian Homologue Apaf-1: A Structural Relationship to the G-proteins (1998)

Cardozo, Timothy J. ; Abagyan, Ruben

Springer

Journal of molecular modeling 4 (1998), S. 83-93

add to mindlist on the mindlist

Details

ISSN: 0948-5023

Keywords: Keywords Structure prediction ; Apoptosis ; Proto-oncogene proteins ; G-proteins ; Caspase

Source: Springer Online Journal Archives 1860-2000

Topics: Chemistry and Pharmacology

Notes: Abstract Apoptosis (programmed cell death, PCD) is a characteristic type of cell death in which a regulated cellular response pathway mediated by cysteine proteases of the caspase family and Bcl-2 family proteins results in ordered and non-inflammatory involution of the cell. The CED-4 protein and its recently identified mammalian homologue Apaf-1 are critical but functionally uncharacterized components of the cell death machinery. We present here a three-dimensional molecular model for the central domain of CED-4, its alternatively spliced transcript (CED-4l) and Apaf-1. A novel protein family is identified and structure prediction for the family identifies a G-protein-like fold with high reliability. The three-dimensional model provides a potential structural explanation for the alternatively spliced variant as well as the known point mutations in CED-4. Regions of the CED-4 and Apaf-1 sequences which may interact with caspases and the Bcl-2 family are proposed. This new information provides a structural molecular framework for the interaction of CED-4-like proteins with the caspases and the Bcl-2 family in the regulation of apoptosis which is analogous to G-protein mediated interactions in well-defined signal transduction pathways.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/s008940050134

Permalink

Library	Location	Call Number	Volume/Issue/Year	Availability

Others were also interested in ...

Paper (German National Licenses)

Fulltext

Electronic Resource

Recognition of distantly related proteins through energy calculations (1994)

Abagyan, Ruben ; Frishman, Dmitrij ; Argos, Patrick

New York, NY : Wiley-Blackwell

Proteins: Structure, Function, and Genetics 19 (1994), S. 132-140

add to mindlist on the mindlist

Details

ISSN: 0887-3585

Keywords: distant protein folds ; sequence homology ; database searching ; profile analysis ; protein structure comparison ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Medicine

Notes: A new method to detect remote relationships between protein sequences and known three-dimensional structures based on direct energy calculations and without reliance on statistics has been developed. The likelihood of a residue to occupy a given position on the structural template was represented by an estimate of the stabilization free energy made after explicit prediction of the substituted side chain conformation. The profile matrix derived from these energy values and modified by increasing the residue self-exchange values successfully predicted compatibility of heatshock protein and globin sequences with the three-dimensional structures of actin and phycocyanin, respectively, from a full protein sequence databank search. The high sensitivity of the method makes it a unique tool for predicting the three-dimensional fold for the rapidly growing number of protein sequences. © 1994 Wiley-Liss, Inc.

Additional Material: 4 Ill.