Investigations of Ramachandran disallowed conformations in protein domain families


Autoria(s): Lakshmi, B; Ramakrishnan, C; Archunan, G; Sowdhamini, R; Srinivasan, N
Data(s)

2014

Resumo

In peptide and protein structures, occurrence of (phi,psi.) angles in the disallowed region of the Ramachandran map almost always suggests local regions of error or poor accuracy. However, very rarely genuine disallowed conformations occur as noted in the current study in proteins of known structure available at ultra-high resolution (<= 1.2 (A) over circle). In the current work, extent of conservation of genuine disallowed conformations in homologous proteins of known structures has been analyzed. From a dataset of 124 protein domain families, with structure of at least one constituent member in each family available at a resolution of 1.2 (A) over circle or better, we have analyzed the conservation of 221 disallowed conformations. It is observed that the disallowed conformation is only moderately conservedin protein domain families. In the gross dataset no particular residue type adopting disallowed conformation elicit high conservation of residue type though there are alignment positions in the dataset with complete conservation of both the residue type and the disallowed conformation. Conserved disallowed conformation in protein domain families play biologically significant role in roughly 50% of the cases. The residues with the disallowed conformation or its flanking residues are often located within or around the functional site of the protein. (C) 2013 Elsevier B.V. All rights reserved.

Formato

application/pdf

Identificador

http://eprints.iisc.ernet.in/48547/1/int_jou_bio_mac_63_119_2014.pdf

Lakshmi, B and Ramakrishnan, C and Archunan, G and Sowdhamini, R and Srinivasan, N (2014) Investigations of Ramachandran disallowed conformations in protein domain families. In: INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 63 . pp. 119-125.

Publicador

ELSEVIER SCIENCE BV

Relação

http://dx.doi.org/10.1016/j.ijbiomac.2013.10.032

http://eprints.iisc.ernet.in/48547/

Palavras-Chave #Molecular Biophysics Unit
Tipo

Journal Article

PeerReviewed