Coupled folding and binding with alpha-helix-forming molecular recognition elements.

@article{citeulike:611175, abstract = {Many protein-protein and protein-nucleic acid interactions involve coupled folding and binding of at least one of the partners. Here, we propose a protein structural element or feature that mediates the binding events of initially disordered regions. This element consists of a short region that undergoes coupled binding and folding within a longer region of disorder. We call these features "molecular recognition elements" (MoREs). Examples of MoREs bound to their partners can be found in the alpha-helix, beta-strand, polyproline II helix, or irregular secondary structure conformations, and in various mixtures of the four structural forms. Here we describe an algorithm that identifies regions having propensities to become alpha-helix-forming molecular recognition elements (alpha-MoREs) based on a discriminant function that indicates such regions while giving a low false-positive error rate on a large collection of structured proteins. Application of this algorithm to databases of genomics and functionally annotated proteins indicates that alpha-MoREs are likely to play important roles protein-protein interactions involved in signaling events.}, address = {Molecular Kinetics Inc., 6201 La Pas Trail, Suite 160, Indianapolis, Indiana 46268, USA.}, author = {Oldfield, C. J. and Cheng, Y. and Cortese, M. S. and Romero, P. and Uversky, V. N. and Dunker, A. K. }, citeulike-article-id = {611175}, doi = {10.1021/bi050736e}, issn = {0006-2960}, journal = {Biochemistry}, keywords = {function}, month = {September}, number = {37}, pages = {12454--12470}, posted-at = {2006-05-02 08:10:15}, priority = {2}, title = {Coupled folding and binding with alpha-helix-forming molecular recognition elements.}, url = {http://dx.doi.org/10.1021/bi050736e}, volume = {44}, year = {2005} }

TY - JOUR ID - citeulike:611175 L3 - citeulike-article-id:611175 TI - Coupled folding and binding with alpha-helix-forming molecular recognition elements. JF - Biochemistry VL - 44 IS - 37 SP - 12454 EP - 12470 AD - Molecular Kinetics Inc., 6201 La Pas Trail, Suite 160, Indianapolis, Indiana 46268, USA. SN - 0006-2960 N2 - Many protein-protein and protein-nucleic acid interactions involve coupled folding and binding of at least one of the partners. Here, we propose a protein structural element or feature that mediates the binding events of initially disordered regions. This element consists of a short region that undergoes coupled binding and folding within a longer region of disorder. We call these features "molecular recognition elements" (MoREs). Examples of MoREs bound to their partners can be found in the alpha-helix, beta-strand, polyproline II helix, or irregular secondary structure conformations, and in various mixtures of the four structural forms. Here we describe an algorithm that identifies regions having propensities to become alpha-helix-forming molecular recognition elements (alpha-MoREs) based on a discriminant function that indicates such regions while giving a low false-positive error rate on a large collection of structured proteins. Application of this algorithm to databases of genomics and functionally annotated proteins indicates that alpha-MoREs are likely to play important roles protein-protein interactions involved in signaling events. KW - function AU - Oldfield, CJ AU - Cheng, Y AU - Cortese, MS AU - Romero, P AU - Uversky, VN AU - Dunker, AK PY - 2005/09/20/ UR - http://dx.doi.org/10.1021/bi050736e ER -