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Structure and catalytic mechanism of human protein tyrosine phosphatome
- Kim, Seung Jun;
- Ryu, Seong Eon
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20초록
Together with protein tyrosine kinases (PTKs), protein tyrosine phosphatases (PTPs) serve as hallmarks in cellular signal transduction by controlling the reversible phosphorylation of their substrates. The human genome is estimated to encode more than 100 PTPs, which can be divided into eleven sub-groups according to their structural and functional characteristics. All the crystal structures of catalytic domains of sub-groups have been elucidated, enabling us to understand their precise catalytic mechanism and to compare their structures across all sub-groups. In this review, I describe the structure and mechanism of catalytic domains of PTPs in the structural context.
키워드
Classical PTP; Crystal structure; Dual specificity PTP; Eyes absent; Protein tyrosine phosphatase (PTP); CRYSTAL-STRUCTURE; PHOSPHOINOSITIDE PHOSPHATASE; EYES ABSENT; DOMAIN; SPECIFICITY; INSIGHTS; ACTIVATION; PRL-1; PHOSPHORYLATION; RECOGNITION
- 제목
- Structure and catalytic mechanism of human protein tyrosine phosphatome
- 저자
- Kim, Seung Jun; Ryu, Seong Eon
- 발행일
- 2012-12
- 유형
- Review
- 저널명
- BMB Reports
- 권
- 45
- 호
- 12
- 페이지
- 693 ~ 699