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PDBsum entry 6tpu
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Cell adhesion
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PDB id
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6tpu
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PDB id:
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| Name: |
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Cell adhesion
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Title:
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Crystal structures of fniii domain three and four of the human leucocyte common antigen-related protein, lar
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Structure:
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Receptor-type tyrosine-protein phosphatase f. Chain: a, b. Synonym: leukocyte common antigen related,lar. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: ptprf, lar. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.55Å
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R-factor:
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0.166
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R-free:
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0.193
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Authors:
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J.P.Vilstrup,S.S.Thirup,A.Simonsen,T.Birkefeldt,D.Strandbygaard
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Key ref:
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J.Vilstrup
et al.
(2020).
Crystal and solution structures of fragments of the human leucocyte common antigen-related protein.
Acta Crystallogr D Struct Biol,
76,
406-417.
PubMed id:
DOI:
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Date:
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14-Dec-19
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Release date:
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13-May-20
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PROCHECK
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Headers
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References
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P10586
(PTPRF_HUMAN) -
Receptor-type tyrosine-protein phosphatase F from Homo sapiens
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Seq:
Struc:
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1907 a.a.
194 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class:
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E.C.3.1.3.48
- protein-tyrosine-phosphatase.
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Reaction:
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O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphate
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O-phospho-L-tyrosyl-[protein]
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+
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H2O
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=
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L-tyrosyl-[protein]
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+
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phosphate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Acta Crystallogr D Struct Biol
76:406-417
(2020)
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PubMed id:
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Crystal and solution structures of fragments of the human leucocyte common antigen-related protein.
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J.Vilstrup,
A.Simonsen,
T.Birkefeldt,
D.Strandbygård,
J.Lyngsø,
J.S.Pedersen,
S.Thirup.
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ABSTRACT
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Leucocyte common antigen-related protein (LAR) is a post-synaptic type I
transmembrane receptor protein that is important for neuronal functionality and
is genetically coupled to neuronal disorders such as attention deficit
hyperactivity disorder (ADHD). To understand the molecular function of LAR,
structural and biochemical studies of protein fragments derived from the
ectodomain of human LAR have been performed. The crystal structure of a fragment
encompassing the first four FNIII domains (LARFN1-4) showed a
characteristic L shape. SAXS data suggested limited flexibility within
LARFN1-4, while rigid-body refinement of the SAXS data using the
X-ray-derived atomic model showed a smaller angle between the domains defining
the L shape compared with the crystal structure. The capabilities of the
individual LAR fragments to interact with heparin was examined using microscale
thermophoresis and heparin-affinity chromatography. The results showed that the
three N-terminal immunoglobulin domains (LARIg1-3) and the four
C-terminal FNIII domains (LARFN5-8) both bound heparin, while
LARFN1-4 did not. The low-molecular-weight heparin drug Innohep
induced a shift in hydrodynamic volume as assessed by size-exclusion
chromatography of LARIg1-3 and LARFN5-8, while the
chemically defined pentameric heparin drug Arixtra did not. Together, the
presented results suggest the presence of an additional heparin-binding site in
human LAR.
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