Analysis of molecular recognition features (MoRFs).

Analysis of molecular recognition features (MoRFs). Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Analysis of molecular recognition features (MoRFs). Abstract Text:

Amrita Mohan,Christopher J Oldfield,Predrag Radivojac,Vladimir Vacic,Marc S Cortese,A Keith Dunker,Vladimir N Uversky,

Several proteomic studies in the last decade revealed that many proteins are either completely disordered or possess long structurally flexible regions. Many such regions were shown to be of functional importance, often allowing a protein to interact with a large number of diverse partners. Parallel to these findings, during the last five years structural bioinformatics has produced an explosion of results regarding protein-protein interactions and their importance for cell signaling. We studied the occurrence of relatively short (10-70 residues), loosely structured protein regions within longer, largely disordered sequences that were characterized as bound to larger proteins. We call these regions molecular recognition features (MoRFs, also known as molecular recognition elements, MoREs). Interestingly, upon binding to their partner(s), MoRFs undergo disorder-to-order transitions. Thus, in our interpretation, MoRFs represent a class of disordered region that exhibits molecular recognition and binding functions. This work extends previous research showing the importance of flexibility and disorder for molecular recognition. We describe the development of a database of MoRFs derived from the RCSB Protein Data Bank and present preliminary results of bioinformatics analyses of these sequences. Based on the structure adopted upon binding, at least three basic types of MoRFs are found: alpha-MoRFs, beta-MoRFs, and iota-MoRFs, which form alpha-helices, beta-strands, and irregular secondary structure when bound, respectively. Our data suggest that functionally significant residual structure can exist in MoRF regions prior to the actual binding event. The contribution of intrinsic protein disorder to the nature and function of MoRFs has also been addressed. The results of this study will advance the understanding of protein-protein interactions and help towards the future development of useful protein-protein binding site predictors.

Analysis of molecular recognition features (MoRFs). Publishing Authors By Initials

A Mohan,CJ Oldfield,P Radivojac,V Vacic,MS Cortese,AK Dunker,VN Uversky,

For similar abstracts research abstracts see: abstracts research

PUBMED ID PMID:

MEDLINE DATE:

Analysis of molecular recognition features (MoRFs). Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of molecular biology

VOLUME: 362

Page Numbers: 1043-59

Journal Abbreviation:

ISSN: 0022-2836

DAY: 4

MONTH: 08

YEAR: 2006

Analysis of molecular recognition features (MoRFs). Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985088

Analysis of molecular recognition features (MoRFs). Keywords Mesh Terms:

KEYWORDS:

MESH TERMS:

Chemical & Substance for Abstract: Analysis of molecular recognition features (MoRFs). Information

Substance Name:

Registry Number:

Grant and Affiliation Information for Analysis of molecular recognition features (MoRFs).

AFFILIATION: School of Informatics, Indiana University, Bloomington, IN 47408, USA.

Country: England

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Mol Biol

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Analysis of molecular recognition features MoRFs Related Publications

• Amyloidogenesis of natively unfolded proteins.
• Analysis of molecular recognition features (MoRFs).
• Effect of methionine oxidation on the structural properties, conformational stability, and aggregation of immunoglobulin light chain LEN.
• Functional anthology of intrinsic disorder. 2. Cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated with long disordered regions.
• Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins.
• Guiding protein aggregation with macromolecular crowding.
• Intrinsic disorder in pathogenic and non-pathogenic microbes: discovering and analyzing the unfoldomes of early-branching eukaryotes.
• Nanoimaging in protein-misfolding and -conformational diseases.
• Protein intrinsic disorder toolbox for comparative analysis of viral proteins.
• Signal transduction via unstructured protein conduits.
• Structural Characteristics of alpha-Synuclein Oligomers Stabilized by the Flavonoid Baicalein.
• The effect of membranes on the in vitro fibrillation of an amyloidogenic light-chain variable-domain SMA.
• The unfoldomics decade: an update on intrinsically disordered proteins.
• alpha-Synuclein Misfolding and Neurodegenerative Diseases.