Dynamics and Mechanism of Substrate Recognition by Matrix Metalloproteases

Ivan E. Collier; Gregory I. Goldberg

doi:10.1002/9781118772287.ch2

Dynamics and Mechanism of Substrate Recognition by Matrix Metalloproteases

Ivan E. Collier, Gregory I. Goldberg

Division of Dermatology

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

5 Scopus citations

Abstract

This chapter focuses on extracellular matrix (ECM) metalloproteinases MMP-1, MMP-2, MMP-9, and MMP-14 (MT1 MMP) and their interactions with substrate. MMP-1, MMP-2, and MMP-9 are tethered in periplasmic space while MT1-MMP is a trans-membrane proteinase. The enzymes were found tightly associated with ECM and collagen in particular. The investigation of MMP-2 binding to gelatin-coated surfaces produced a number of seemingly paradoxical observations. The uniqueness of the mammalian collagenase cleavage site in native triple helical collagen (THC) types I, II, and III lies in the primary amino acid sequence and also in unique physico-chemical properties of the surrounding area. Brownian motion of MMP-1 is interrupted by the stochastic pauses of type I with exponential time of escape distribution and type II pauses at "hot spot" binding sites that occur at 1. 3 and/or 1. 5 μm intervals along the fibril.

Original language	English
Title of host publication	Matrix Metalloproteinase Biology
Publisher	wiley
Pages	23-40
Number of pages	18
ISBN (Electronic)	9781118772287
ISBN (Print)	9781118772324
DOIs	https://doi.org/10.1002/9781118772287.ch2
State	Published - May 29 2015

Keywords

Brownian motion
Cleavage-diffusion coupling
Collagenase
Gelatin
Matrix metalloproteases
Periplasmic space
Proteinase
Substrate recognition
Surface diffusion
Triple helical collagen

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title = "Dynamics and Mechanism of Substrate Recognition by Matrix Metalloproteases",

abstract = "This chapter focuses on extracellular matrix (ECM) metalloproteinases MMP-1, MMP-2, MMP-9, and MMP-14 (MT1 MMP) and their interactions with substrate. MMP-1, MMP-2, and MMP-9 are tethered in periplasmic space while MT1-MMP is a trans-membrane proteinase. The enzymes were found tightly associated with ECM and collagen in particular. The investigation of MMP-2 binding to gelatin-coated surfaces produced a number of seemingly paradoxical observations. The uniqueness of the mammalian collagenase cleavage site in native triple helical collagen (THC) types I, II, and III lies in the primary amino acid sequence and also in unique physico-chemical properties of the surrounding area. Brownian motion of MMP-1 is interrupted by the stochastic pauses of type I with exponential time of escape distribution and type II pauses at {"}hot spot{"} binding sites that occur at 1. 3 and/or 1. 5 μm intervals along the fibril.",

keywords = "Brownian motion, Cleavage-diffusion coupling, Collagenase, Gelatin, Matrix metalloproteases, Periplasmic space, Proteinase, Substrate recognition, Surface diffusion, Triple helical collagen",

author = "Collier, {Ivan E.} and Goldberg, {Gregory I.}",

year = "2015",

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doi = "10.1002/9781118772287.ch2",

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AU - Collier, Ivan E.

AU - Goldberg, Gregory I.

PY - 2015/5/29

Y1 - 2015/5/29

N2 - This chapter focuses on extracellular matrix (ECM) metalloproteinases MMP-1, MMP-2, MMP-9, and MMP-14 (MT1 MMP) and their interactions with substrate. MMP-1, MMP-2, and MMP-9 are tethered in periplasmic space while MT1-MMP is a trans-membrane proteinase. The enzymes were found tightly associated with ECM and collagen in particular. The investigation of MMP-2 binding to gelatin-coated surfaces produced a number of seemingly paradoxical observations. The uniqueness of the mammalian collagenase cleavage site in native triple helical collagen (THC) types I, II, and III lies in the primary amino acid sequence and also in unique physico-chemical properties of the surrounding area. Brownian motion of MMP-1 is interrupted by the stochastic pauses of type I with exponential time of escape distribution and type II pauses at "hot spot" binding sites that occur at 1. 3 and/or 1. 5 μm intervals along the fibril.

AB - This chapter focuses on extracellular matrix (ECM) metalloproteinases MMP-1, MMP-2, MMP-9, and MMP-14 (MT1 MMP) and their interactions with substrate. MMP-1, MMP-2, and MMP-9 are tethered in periplasmic space while MT1-MMP is a trans-membrane proteinase. The enzymes were found tightly associated with ECM and collagen in particular. The investigation of MMP-2 binding to gelatin-coated surfaces produced a number of seemingly paradoxical observations. The uniqueness of the mammalian collagenase cleavage site in native triple helical collagen (THC) types I, II, and III lies in the primary amino acid sequence and also in unique physico-chemical properties of the surrounding area. Brownian motion of MMP-1 is interrupted by the stochastic pauses of type I with exponential time of escape distribution and type II pauses at "hot spot" binding sites that occur at 1. 3 and/or 1. 5 μm intervals along the fibril.

KW - Brownian motion

KW - Cleavage-diffusion coupling

KW - Collagenase

KW - Gelatin

KW - Matrix metalloproteases

KW - Periplasmic space

KW - Proteinase

KW - Substrate recognition

KW - Surface diffusion

KW - Triple helical collagen

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U2 - 10.1002/9781118772287.ch2

DO - 10.1002/9781118772287.ch2

M3 - Chapter

AN - SCOPUS:85015980231

SN - 9781118772324

SP - 23

EP - 40

BT - Matrix Metalloproteinase Biology

PB - wiley

ER -

Dynamics and Mechanism of Substrate Recognition by Matrix Metalloproteases

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Keywords

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