4n5u | pdb_00004n5u
From Proteopedia
Crystal structure of the 4th FN3 domain of human Protein Tyrosine phosphatase, receptor type F [PSI-NYSGRC-006240]
Function
[PTPRF_HUMAN] Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase).[1] The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one.[2]
About this Structure
4n5u is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- ↑ Nam HJ, Poy F, Krueger NX, Saito H, Frederick CA. Crystal structure of the tandem phosphatase domains of RPTP LAR. Cell. 1999 May 14;97(4):449-57. PMID:10338209
- ↑ Nam HJ, Poy F, Krueger NX, Saito H, Frederick CA. Crystal structure of the tandem phosphatase domains of RPTP LAR. Cell. 1999 May 14;97(4):449-57. PMID:10338209
Proteopedia Page Contributors and Editors (what is this?)
Categories:
- Homo sapiens
- Protein-tyrosine-phosphatase
- Almo, S C.
- Attonito, J.
- Banu, R.
- Bhosle, R.
- Calarese, D A.
- Casadevall, A.
- Celikgil, A.
- Chamala, S.
- Chan, M K.
- Chowdhury, S.
- Fiser, A.
- Garforth, S J.
- Glenn, A S.
- Hillerich, B.
- IFN, Atoms-to-Animals:.The Immune Function Network.
- Khafizov, K.
- Kumar, P R.
- Love, J D.
- NYSGRC, New York Structural Genomics Research Consortium.
- Patel, H.
- Patel, R.
- Seidel, R D.
- Smith, B.
- Stead, M.
- Toro, R.
- Hydrolase
- Internal fn3 domain
- Psi-biology
- Structural genomic
