全长基质金属蛋白酶-1（MMP-1）的结构域间灵活性
Interdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1).
作者信息
Bertini Ivano, Fragai Marco, Luchinat Claudio, Melikian Maxime, Mylonas Efstratios, Sarti Niko, Svergun Dmitri I
机构信息
Magnetic Resonance Center, University of Florence, Sesto Fiorentino, Italy.
出版信息
J Biol Chem. 2009 May 8;284(19):12821-8. doi: 10.1074/jbc.M809627200. Epub 2009 Mar 12.
Abstract
The presence of extensive reciprocal conformational freedom between the catalytic and the hemopexin-like domains of full-length matrix metalloproteinase-1 (MMP-1) is demonstrated by NMR and small angle x-ray scattering experiments. This finding is discussed in relation to the essentiality of the hemopexin-like domain for the collagenolytic activity of MMP-1. The conformational freedom experienced by the present system, having the shortest linker between the two domains, when compared with similar findings on MMP-12 and MMP-9 having longer and the longest linker within the family, respectively, suggests this type of conformational freedom to be a general property of all MMPs.
摘要
核磁共振（NMR）和小角X射线散射实验表明，全长基质金属蛋白酶-1（MMP-1）的催化结构域和血色素结合素样结构域之间存在广泛的相互构象自由度。结合血色素结合素样结构域对MMP-1胶原分解活性的必要性，对这一发现进行了讨论。与该家族中分别具有较长和最长连接子的MMP-12和MMP-9的类似发现相比，本系统（两个结构域之间具有最短连接子）所经历的构象自由度表明，这种构象自由度是所有基质金属蛋白酶的普遍特性。
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