CC+: a relational database of coiled-coil structures

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CC+: a relational database of coiled-coil structures

UNLABELLED We introduce the CC+ DATABASE, a detailed, searchable repository of coiled-coil assignments, which is freely available at http://coiledcoils.chm.bris.ac.uk/ccplus. Coiled coils were identified using the program SOCKET, which locates coiled coils based on knobs-into-holes packing of side chains between alpha-helices. A method for determining the overall sequence identity of coiled-coi...

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Solving coiled-coil protein structures

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High-resolution structures of a heterochiral coiled coil.

Interactions between polypeptide chains containing amino acid residues with opposite absolute configurations have long been a source of interest and speculation, but there is very little structural information for such heterochiral associations. The need to address this lacuna has grown in recent years because of increasing interest in the use of peptides generated from d amino acids (d peptide...

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A periodic table of coiled-coil protein structures.

Coiled coils are protein structure domains with two or more alpha-helices packed together via interlacing of side chains known as knob-into-hole packing. We analysed and classified a large set of coiled-coil structures using a combination of automated and manual methods. This led to a systematic classification that we termed a "periodic table of coiled coils," which we have made available at ht...

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Routine phasing of coiled-coil protein crystal structures with AMPLE

Coiled-coil protein folds are among the most abundant in nature. These folds consist of long wound α-helices and are architecturally simple, but paradoxically their crystallographic structures are notoriously difficult to solve with molecular-replacement techniques. The program AMPLE can solve crystal structures by molecular replacement using ab initio search models in the absence of an existen...

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ژورنال

عنوان ژورنال: Nucleic Acids Research

سال: 2009

ISSN: 0305-1048,1362-4962

DOI: 10.1093/nar/gkn675