Ontology highlight
ABSTRACT:
SUBMITTER: Zhang Y
PROVIDER: S-EPMC4420519 | biostudies-literature | 2015 May
REPOSITORIES: biostudies-literature
Zhang Yugang Y Cao Huaiqing H Liu Zhirong Z
Protein science : a publication of the Protein Society 20150224 5
To assess the potential of intrinsically disordered proteins (IDPs) as drug design targets, we have analyzed the ligand-binding cavities of two datasets of IDPs (containing 37 and 16 entries, respectively) and compared their properties with those of conventional ordered (folded) proteins. IDPs were predicted to possess more binding cavity than ordered proteins at similar length, supporting the proposed advantage of IDPs economizing genome and protein resources. The cavity number has a wide distr ...[more]