Active site specificity profiling of the matrix metalloproteinase family: Proteomic identification of 4300 cleavage sites by nine MMPs explored with structural and synthetic peptide cleavage analyses
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- 作者：Ulrich Eckhard1 ; &Dagger ; ; Pitter F. Huesgen1 ; 2 ; &Dagger ; ; Oliver Schilling1 ; 3 ; &Dagger ; ; Caroline L. Bellac1 ; 4 ; # ; Georgina S. Butler1 ; # ; Jennifer H. Cox1 ; 5 ; # ; Antoine Dufour1 ; # ; Verena Goebeler1 ; # ; Reinhild Kappelhoff1 ; # ; Ulrich auf dem Keller1 ; 6 ; # ; Theo Klein1 ; # ; Philipp F. Lange1 ; 7 ; # ; Giada Marino1 ; # ; Charlotte J. Morrison1 ; 8 ; # ; Anna Prudova1 ; # ; David Rodriguez1 ; 9 ; # ; Amanda E. Starr1 ; 10 ; # ; Yili Wang1 ; # ; Christopher M. Overall1 ; 11 ; chris.overall@ubc.ca" class="auth_mail" title="E-mail the corresponding author
- 关键词：MMPs ; Specificity profiling ; Proteomics ; Quenched-fluorescent peptides ; PICS ; Peptide docking
- 刊名：Matrix Biology
- 出版年：2016
- 出版时间：January 2016
- 年：2016
- 卷：49
- 期：Complete
- 页码：37-60
- 全文大小：4309 K
文摘
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Identification of > 4300 cleavage sites creates a family-wide MMP portrayal.
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Subtle active-site specificity divergences demarcate individual MMP-family members.
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Negative cooperativity ties the hallmark specificity features P3-Pro and P1′-Leu.
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P1-Asn and nonprime side flexibility emerge as crucial specificity features.
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Heat maps and iceLogos mask subsite cooperativity.