.png){kind=icon}
返回
Engineering of selective TIMPs
.png){kind=icon}
PRE
AI
DOI：10.1111/j.1749-6632.1999.tb07670.x.png)
.png){kind=icon}
原文求助.png){kind=icon}
分享.png){kind=icon}
收藏
摘要
En 中文
Differences in proteinase susceptibility between free TIMP-1 and the TIMP-1-MMP-3 complex and mutagenesis studies suggested that the residues around the disulfide bond between Cys1 and Cys70 in TIMP-1 may interact with MMPs. The crystal structure of the complex between TIMP-1 and the catalytic domain of MMP-3 has revealed that the alpha-amino group of Cys1 bidentately chelates the catalytic zinc of MMP-3 and the Thr2 side chain occupies the S-1' pocket. Generation of the N-terminal domain of TIMP-1 (N-TIMP-1) variants with 15 different amino acid substitutions for Thr2 has indicated that the nature of the side chain of residue 2 has a major effect on the affinity of N-TIMP-1 for three different MMPs (MMPs-1, -2 and -3). The results also demonstrate that the mode of binding of N-TIMP-1 residue 2 differs from the binding of the P-1' residue of a peptide substrate.
Keyword:
HUMAN TISSUE INHIBITOR
AMINO-TERMINAL DOMAIN
PROGELATINASE-A
MATRIX METALLOPROTEINASE
4-AMINOPHENYLMERCURIC ACETATE
SEQUENCE SPECIFICITIES
NEUTROPHIL ELASTASE
ACTIVE DOMAIN
GELATINASE-A
CELL-SURFACE
AI总结
对已上传原文的论文进行重点信息的提取，主要内容包括：简要概述、研究摘要、背景介绍、关键亮点、图文解析、展望与总结。
期刊
暂无期刊信息
机构
暂无机构信息
引用论文
Progesterone interaction with estrogen and antiestrogen in the rat uterus — receptor effects.png)
Steroids
SteroidsIF0
PREAI
分享收藏
Effects of Twin Boundary on Tensile Properties and Deformation Mechanism of Ni–Co Alloy Nanopillars
PREAI
分享收藏Folding and characterization of the amino-terminal domain of human tissue inhibitor of metalloproteinases-1 (TIMP-1) expressed at high yield in E-coliFEBS LETTERS
FEBS LETTERSIF3
PREAI
分享收藏
查看更多内容