PIC: Protein Interactions Calculator

被引:750
作者
Tina, K. G. [1 ]
Bhadra, R. [1 ]
Srinivasan, N. [1 ]
机构
[1] Indian Inst Sci, Mol Biophys Unit, Bangalore 560012, Karnataka, India
关键词
D O I
10.1093/nar/gkm423
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Interactions within a protein structure and interactions between proteins in an assembly are essential considerations in understanding molecular basis of stability and functions of proteins and their complexes. There are several weak and strong interactions that render stability to a protein structure or an assembly. Protein Interactions Calculator (PIC) is a server which, given the coordinate set of 3D structure of a protein or an assembly, computes various interactions such as disulphide bonds, interactions between hydrophobic residues, ionic interactions, hydrogen bonds, aromatic aromatic interactions, aromatic-sulphur interactions and cation-pi interactions within a protein or between proteins in a complex. Interactions are calculated on the basis of standard, published criteria. The identified interactions between residues can be visualized using a RasMol and Jmol interface. The advantage with PIC server is the easy availability of inter-residue interaction calculations in a single site. It also determines the accessible surface area and residue-depth, which is the distance of a residue from the surface of the protein. User can also recognize specific kind of interactions, such as apolar-apolar residue interactions or ionic interactions, that are formed between buried or exposed residues or near the surface or deep inside.
引用
收藏
页码:W473 / W476
页数:4
相关论文
共 35 条
[1]   Three-dimensional structure of the water-insoluble protein crambin in doidecylphosphocholine micelles and its minimal solvent-exposed surface [J].
Ahn, HC ;
Juranic, N ;
Macura, S ;
Markley, JL .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2006, 128 (13) :4398-4404
[2]   Sequence determinants of a conformational switch in a protein structure [J].
Anderson, TA ;
Cordes, MHJ ;
Sauer, RT .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (51) :18344-18349
[3]   NCI: a server to identify non-canonical interactions in protein structures [J].
Babu, MM .
NUCLEIC ACIDS RESEARCH, 2003, 31 (13) :3345-3348
[4]   A dissection of specific and non-specific protein - Protein interfaces [J].
Bahadur, RP ;
Chakrabarti, P ;
Rodier, F ;
Janin, J .
JOURNAL OF MOLECULAR BIOLOGY, 2004, 336 (04) :943-955
[5]   Tolerance to the substitution of buried apolar residues by charged residues in the homologous protein structures [J].
Balaji, S ;
Aruna, S ;
Srinivasan, N .
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2003, 53 (04) :783-791
[6]   ION-PAIRS IN PROTEINS [J].
BARLOW, DJ ;
THORNTON, JM .
JOURNAL OF MOLECULAR BIOLOGY, 1983, 168 (04) :867-885
[7]   Conserved spatially interacting motifs of protein superfamilies: Application to fold recognition and function annotation of genome data [J].
Bhaduri, A ;
Ravishankar, R ;
Sowdhamini, R .
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2004, 54 (04) :657-670
[8]   The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases [J].
Brown, NR ;
Noble, MEM ;
Endicott, JA ;
Johnson, LN .
NATURE CELL BIOLOGY, 1999, 1 (07) :438-443
[9]   AROMATIC-AROMATIC INTERACTION - A MECHANISM OF PROTEIN-STRUCTURE STABILIZATION [J].
BURLEY, SK ;
PETSKO, GA .
SCIENCE, 1985, 229 (4708) :23-28
[10]   Residue depth: a novel parameter for the analysis of protein structure and stability [J].
Chakravarty, S ;
Varadarajan, R .
STRUCTURE WITH FOLDING & DESIGN, 1999, 7 (07) :723-732