New structures of allosteric proteins revealing remarkable conformational changes

Andrea Mattevi; Menico Rizzi; Martino Bolognesi

doi:10.1016/S0959-440X(96)80013-3

New structures of allosteric proteins revealing remarkable conformational changes

Andrea Mattevi
, Menico Rizzi
, Martino Bolognesi

Research output: Contribution to journal › Article › peer-review

Abstract

New three-dimensional structures of allosteric proteins reveal they have a flexible architecture that is instrumental to the regulation of protein function. Highlights are the structures of GroEL, pyruvate kinase, D-9-phosphoglycerate dehydrogenase and the acetylcholine receptor. Furthermore, significant progress in understanding the nature of the intermediates involved in an allosteric reaction has been achieved through recent spectroscopic and crystallographic studies on haemoglobin.

Original language	English
Pages (from-to)	824-829
Number of pages	6
Journal	Current Opinion in Structural Biology
Volume	6
Issue number	6
DOIs	https://doi.org/10.1016/S0959-440X(96)80013-3
Publication status	Published - Dec 1996
Externally published	Yes

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10.1016/S0959-440X(96)80013-3

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title = "New structures of allosteric proteins revealing remarkable conformational changes",

abstract = "New three-dimensional structures of allosteric proteins reveal they have a flexible architecture that is instrumental to the regulation of protein function. Highlights are the structures of GroEL, pyruvate kinase, D-9-phosphoglycerate dehydrogenase and the acetylcholine receptor. Furthermore, significant progress in understanding the nature of the intermediates involved in an allosteric reaction has been achieved through recent spectroscopic and crystallographic studies on haemoglobin.",

author = "Andrea Mattevi and Menico Rizzi and Martino Bolognesi",

year = "1996",

month = dec,

doi = "10.1016/S0959-440X(96)80013-3",

language = "English",

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T1 - New structures of allosteric proteins revealing remarkable conformational changes

AU - Mattevi, Andrea

AU - Rizzi, Menico

AU - Bolognesi, Martino

PY - 1996/12

Y1 - 1996/12

N2 - New three-dimensional structures of allosteric proteins reveal they have a flexible architecture that is instrumental to the regulation of protein function. Highlights are the structures of GroEL, pyruvate kinase, D-9-phosphoglycerate dehydrogenase and the acetylcholine receptor. Furthermore, significant progress in understanding the nature of the intermediates involved in an allosteric reaction has been achieved through recent spectroscopic and crystallographic studies on haemoglobin.

AB - New three-dimensional structures of allosteric proteins reveal they have a flexible architecture that is instrumental to the regulation of protein function. Highlights are the structures of GroEL, pyruvate kinase, D-9-phosphoglycerate dehydrogenase and the acetylcholine receptor. Furthermore, significant progress in understanding the nature of the intermediates involved in an allosteric reaction has been achieved through recent spectroscopic and crystallographic studies on haemoglobin.

UR - https://www.scopus.com/pages/publications/0030444081

U2 - 10.1016/S0959-440X(96)80013-3

DO - 10.1016/S0959-440X(96)80013-3

M3 - Article

SN - 0959-440X

VL - 6

SP - 824

EP - 829

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

IS - 6

ER -

New structures of allosteric proteins revealing remarkable conformational changes

Abstract

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