Phospho3D 2.0: an enhanced database of three-dimensional structures of phosphorylation sites

نویسندگان

  • Andreas Zanzoni
  • Daniel Carbajo
  • Francesca Diella
  • Pier Federico Gherardini
  • Anna Tramontano
  • Manuela Helmer-Citterich
  • Allegra Via
چکیده

Phospho3D is a database of three-dimensional (3D) structures of phosphorylation sites (P-sites) derived from the Phospho.ELM database, which also collects information on the residues surrounding the P-site in space (3D zones). The database also provides the results of a large-scale structural comparison of the 3D zones versus a representative dataset of structures, thus associating to each P-site a number of structurally similar sites. The new version of Phospho3D presents an 11-fold increase in the number of 3D sites and incorporates several additional features, including new structural descriptors, the possibility of selecting non-redundant sets of 3D structures and the availability for download of non-redundant sets of structurally annotated P-sites. Moreover, it features P3Dscan, a new functionality that allows the user to submit a protein structure and scan it against the 3D zones collected in the Phospho3D database. Phospho3D version 2.0 is available at: http://www.phospho3d.org/.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Phospho3D: a database of three-dimensional structures of protein phosphorylation sites

Phosphorylation is the most common protein post-translational modification. Phosphorylated residues (serine, threonine and tyrosine) play critical roles in the regulation of many cellular processes. Since the amount of data produced by screening assays is growing continuously, the development of computational tools for collecting and analysing experimental data has become a pivotal task for unr...

متن کامل

Characteristics Determination of Rheb Gene and Protein in Raini Cashmere Goat

The aim of the present study was todeterminecharacteristics of Rheb gene and protein in Raini Cashmere goat. Comparative analyses of the nucleotide sequences were performed. Open reading frames (ORFs), theoretical molecular weights of deduced polypeptides, the protein isoelectric point, protein characteristics and three-dimensional structures was predicted using online standard softwares. The f...

متن کامل

A simple form of MT impedance tensor analysis to simplify its decomposition to remove the effects of near surface small-scale 3-D conductivity structures

Magnetotelluric (MT) is a natural electromagnetic (EM) technique which is used for geothermal, petroleum, geotechnical, groundwater and mineral exploration. MT is also routinely used for mapping of deep subsurface structures. In this method, the measured regional complex impedance tensor (Z) is substantially distorted by any topographical feature or small-scale near-surface, three-dimensional (...

متن کامل

The feasibility of direct treatment planning via contrast-enhanced computed tomography: an evaluation of dose differences based on the dimensional dose distribution comparison method

Background: We used a MapCHECK software-based dimensional dose distribution comparison method capable of evaluating point-to-point geometrical dose differences in volume to determine whether doses obtained from an enhanced computed tomography (CT)-based treatment plan, which better defines the target regions and organs at risk, differs from doses obtained from plain CT and then evaluated the fe...

متن کامل

PROCARB: A Database of Known and Modelled Carbohydrate-Binding Protein Structures with Sequence-Based Prediction Tools

Understanding of the three-dimensional structures of proteins that interact with carbohydrates covalently (glycoproteins) as well as noncovalently (protein-carbohydrate complexes) is essential to many biological processes and plays a significant role in normal and disease-associated functions. It is important to have a central repository of knowledge available about these protein-carbohydrate c...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره 39  شماره 

صفحات  -

تاریخ انتشار 2011