DIP/Dpr interactions and the evolutionary design of specificity in protein families

Dpr (Defective proboscis extension response) and DIP (Dpr Interacting Proteins) are immunoglobulin-like cell-cell adhesion proteins that form highly specific pairwise interactions, which control synaptic connectivity during Drosophila development. Here, the authors combine a computational approach w...

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Autores principales:	Alina P. Sergeeva, Phinikoula S. Katsamba, Filip Cosmanescu, Joshua J. Brewer, Goran Ahlsen, Seetha Mannepalli, Lawrence Shapiro, Barry Honig
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/13350acddc38455f905089b350c9c95f
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spelling	oai:doaj.org-article:13350acddc38455f905089b350c9c95f2021-12-02T15:39:18ZDIP/Dpr interactions and the evolutionary design of specificity in protein families10.1038/s41467-020-15981-82041-1723https://doaj.org/article/13350acddc38455f905089b350c9c95f2020-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-15981-8https://doaj.org/toc/2041-1723Dpr (Defective proboscis extension response) and DIP (Dpr Interacting Proteins) are immunoglobulin-like cell-cell adhesion proteins that form highly specific pairwise interactions, which control synaptic connectivity during Drosophila development. Here, the authors combine a computational approach with binding affinity measurements and find that DIP/Dpr binding specificity is controlled by negative constraints that interfere with non-cognate binding.Alina P. SergeevaPhinikoula S. KatsambaFilip CosmanescuJoshua J. BrewerGoran AhlsenSeetha MannepalliLawrence ShapiroBarry HonigNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Alina P. Sergeeva Phinikoula S. Katsamba Filip Cosmanescu Joshua J. Brewer Goran Ahlsen Seetha Mannepalli Lawrence Shapiro Barry Honig DIP/Dpr interactions and the evolutionary design of specificity in protein families
description	Dpr (Defective proboscis extension response) and DIP (Dpr Interacting Proteins) are immunoglobulin-like cell-cell adhesion proteins that form highly specific pairwise interactions, which control synaptic connectivity during Drosophila development. Here, the authors combine a computational approach with binding affinity measurements and find that DIP/Dpr binding specificity is controlled by negative constraints that interfere with non-cognate binding.
format	article
author	Alina P. Sergeeva Phinikoula S. Katsamba Filip Cosmanescu Joshua J. Brewer Goran Ahlsen Seetha Mannepalli Lawrence Shapiro Barry Honig
author_facet	Alina P. Sergeeva Phinikoula S. Katsamba Filip Cosmanescu Joshua J. Brewer Goran Ahlsen Seetha Mannepalli Lawrence Shapiro Barry Honig
author_sort	Alina P. Sergeeva
title	DIP/Dpr interactions and the evolutionary design of specificity in protein families
title_short	DIP/Dpr interactions and the evolutionary design of specificity in protein families
title_full	DIP/Dpr interactions and the evolutionary design of specificity in protein families
title_fullStr	DIP/Dpr interactions and the evolutionary design of specificity in protein families
title_full_unstemmed	DIP/Dpr interactions and the evolutionary design of specificity in protein families
title_sort	dip/dpr interactions and the evolutionary design of specificity in protein families
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/13350acddc38455f905089b350c9c95f
work_keys_str_mv	AT alinapsergeeva dipdprinteractionsandtheevolutionarydesignofspecificityinproteinfamilies AT phinikoulaskatsamba dipdprinteractionsandtheevolutionarydesignofspecificityinproteinfamilies AT filipcosmanescu dipdprinteractionsandtheevolutionarydesignofspecificityinproteinfamilies AT joshuajbrewer dipdprinteractionsandtheevolutionarydesignofspecificityinproteinfamilies AT goranahlsen dipdprinteractionsandtheevolutionarydesignofspecificityinproteinfamilies AT seethamannepalli dipdprinteractionsandtheevolutionarydesignofspecificityinproteinfamilies AT lawrenceshapiro dipdprinteractionsandtheevolutionarydesignofspecificityinproteinfamilies AT barryhonig dipdprinteractionsandtheevolutionarydesignofspecificityinproteinfamilies
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DIP/Dpr interactions and the evolutionary design of specificity in protein families

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