The Concise Guide to Pharmacology 2013/14: Overview

The Concise Guide to PHARMACOLOGY 2013/14 provides concise overviews of the key properties of over 2000 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties from the IUPHAR database. The full contents can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.12444/full. This compilation of the major pharmacological targets is divided into seven areas of focus: G protein-coupled receptors, ligand-gated ion channels, ion channels, catalytic receptors, nuclear hormone receptors, transporters and enzymes. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. A new landscape format has easy to use tables comparing related targets. It is a condensed version of material contemporary to late 2013, which is presented in greater detail and constantly updated on the website www.guidetopharmacology.org, superseding data presented in previous Guides to Receptors & Channels. It is produced in conjunction with NC-IUPHAR and provides the official IUPHAR classification and nomenclature for human drug targets, where appropriate. It consolidates information previously curated and displayed separately in IUPHAR-DB and GRAC and provides a permanent, citable, point-in-time record that will survive database updates.

The great proliferation of drug targets in recent years has driven the need to provide a logically-organised synopsis of the nomenclature and pharmacology of these targets. This is the underlying reason for this Guide to PHARMACOLOGY 2013/14, distributed with the British Journal of Pharmacology, and produced in association with NC-IUPHAR, the Nomenclature Committees of the International Union of Basic and Clinical Pharmacology. Our intent is to produce an authoritative but user-friendly publication, which allows a rapid overview of the key properties of a wide range of established or potential pharmacological targets. The aim is to provide information succinctly, so that a newcomer to a particular target group can identify the main elements 'at a glance'. It is not our goal to produce all-inclusive reviews of the targets presented; references to these are included in the Further Reading sections of the entries or, for many targets, the website www.guidetopharmacology.org provides access to more extensive information. The Guide to PHARMACOLOGY 2013/14 presents each entry, typically a circumscribed target class family on, wherever possible, a single page, so as to allow easy access and rapid oversight.
The list of targets present is, in many cases, a comprehensive reflection of the known targets within the particular group. Our philosophy has been to present data on human proteins wherever possible, both in terms of structural information and pharmacology. To this end, the HGNC gene nomenclature and UniProt unique ID are indicated to allow rapid access through free online databases for further information. In a few cases, where structural or pharmacological information is not available for human targets, we have used data from other species, as indicated. A priority in constructing these tables was to present agents which represent the most selective and which are available by donation or from commercial sources, now or in the near future.
The Guide is divided into seven further sections, which comprise pharmacological targets of similar structure/function. These are G protein-coupled receptors, ligand-gated ion channels, ion channels, catalytic receptors, nuclear hormone receptors, transporters and enzymes. In this overview are listed protein targets of pharmacological interest, which are not G protein-coupled receptors, ligand-gated ion channels, ion channels, nuclear hormone receptors, catalytic receptors, transporters or enzymes. In comparison with the Fifth Edition of the Guide to Receptors & Channels [1], we have added a number of new records, expanding the total to include over 2000 protein targets, primarily from increasing the content on transporters and enzymes.
The Editors of the Guide have compiled the individual records, taking advice from many Collaborators (listed on page 1452). Where appropriate, an indication is given of the status of the nomenclature, as proposed by NC-IUPHAR, published in Pharmacological Reviews. Where this guidance is lacking, advice from several prominent, independent experts has generally been obtained to produce an authoritative consensus, which attempts to fit in within the general guidelines from NC-IUPHAR [2]. Tabulated data provide ready comparison of selective agents and probes (radioligands and PET ligands, where available) within a family of targets and additional commentary highlights whether species differences or ligand metabolism are potential confounding factors. We recommend that any citations to information in the Concise Guide are presented in the following format:

Adiponectin receptors
Overview: Adiponectin receptors (provisional nomenclature, ENSFM00500000270960) respond to the 30 kDa complementrelated protein hormone adiponectin (also known as ADIPOQ: adipocyte, C1q and collagen domain-containing protein; ACRP30, adipose most abundant gene transcript 1; apM-1; gelatin-binding protein: Q15848) originally cloned from adipocytes [4]. Although sequence data suggest 7TM domains, immunological evidence indicates that, contrary to typical 7TM topology, the carboxyl terminus is extracellular, while the amino terminus is intracellular [6]. Signalling through these receptors appears to avoid G proteins. Adiponectin receptors appear rather to stimulate protein phosphorylation via AMP-activated protein kinase and MAP kinase pathways [6], possibly through the protein partner APPL1 (adaptor protein, phosphotyrosine interaction, PH domain and leucine zipper containing 1, Q9UKG1 [5]). The adiponectin receptors are a class of proteins (along with membrane progestin receptors), which contain seven sequences of aliphatic amino acids reminiscent of GPCRs, but which are structurally and functionally distinct from that class of receptor.

Fatty acid binding proteins
Overview: Fatty acid-binding proteins are low molecular weight (100-130 aa) chaperones for long chain fatty acids, fatty acyl CoA esters, eicosanoids, retinols, retinoic acids and related metabolites and are usually regarded as being responsible for allowing the otherwise hydrophobic ligands to be mobile in aqueous media. These binding proteins may perform functions extracellularly (e.g. in plasma) or transport these agents; to the nucleus to interact with nuclear receptors (principally PPARs and retinoic acid receptors [16]) or for interaction with metabolic enzymes. Although sequence homology is limited, crystallographic studies suggest conserved 3D structures across the group of binding proteins.