PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25525273-6	2015	We determine the 2.75 A co-crystal structure of the CCM2 PTB domain with a peptide corresponding to KRIT1(NPX(Y/F)3), revealing a Dab-like PTB fold for CCM2 and its interaction with KRIT1(NPX(Y/F)3).	diazobenzenesulfonic acid	130-133	polypyrimidine tract binding protein 1	Homo sapiens	57-60	
25525273-6	2015	We determine the 2.75 A co-crystal structure of the CCM2 PTB domain with a peptide corresponding to KRIT1(NPX(Y/F)3), revealing a Dab-like PTB fold for CCM2 and its interaction with KRIT1(NPX(Y/F)3).	diazobenzenesulfonic acid	130-133	polypyrimidine tract binding protein 1	Homo sapiens	139-142	
22645138-5	2012	Our HADDOCK-derived complex structure model elucidates the molecular mechanism by which tensin2 PTB domain recognizes DLC1 peptide and reveals a PTB-peptide binding mode that is unique in that peptide occupies the binding site opposite to the canonical NPXY motif interaction site with the peptide utilizing a non-canonical binding motif to bind in an extended conformation and that the N-terminal helix, which is unique to some Shc- and Dab-like PTB domains, is required for binding.	diazobenzenesulfonic acid	438-441	polypyrimidine tract binding protein 1	Homo sapiens	96-99	
22645138-5	2012	Our HADDOCK-derived complex structure model elucidates the molecular mechanism by which tensin2 PTB domain recognizes DLC1 peptide and reveals a PTB-peptide binding mode that is unique in that peptide occupies the binding site opposite to the canonical NPXY motif interaction site with the peptide utilizing a non-canonical binding motif to bind in an extended conformation and that the N-terminal helix, which is unique to some Shc- and Dab-like PTB domains, is required for binding.	diazobenzenesulfonic acid	438-441	polypyrimidine tract binding protein 1	Homo sapiens	145-148	
22645138-5	2012	Our HADDOCK-derived complex structure model elucidates the molecular mechanism by which tensin2 PTB domain recognizes DLC1 peptide and reveals a PTB-peptide binding mode that is unique in that peptide occupies the binding site opposite to the canonical NPXY motif interaction site with the peptide utilizing a non-canonical binding motif to bind in an extended conformation and that the N-terminal helix, which is unique to some Shc- and Dab-like PTB domains, is required for binding.	diazobenzenesulfonic acid	438-441	polypyrimidine tract binding protein 1	Homo sapiens	145-148	
18550529-6	2008	Although Fe65-PTB1 has been classified on an evolutionary basis as a Dab-like PTB domain, it contains attributes of other PTB domain subfamilies.	diazobenzenesulfonic acid	69-72	polypyrimidine tract binding protein 1	Homo sapiens	14-18	
15567406-6	2005	In this review, we use structural, evolutionary and functional analysis to divide PTB domains into three groups represented by phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like and phosphotyrosine-independent Dab-like PTBs, with the Dab-like PTB domains representing nearly 75% of proteins encoding PTB domains.	diazobenzenesulfonic acid	230-233	polypyrimidine tract binding protein 1	Homo sapiens	82-85	
15567406-6	2005	In this review, we use structural, evolutionary and functional analysis to divide PTB domains into three groups represented by phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like and phosphotyrosine-independent Dab-like PTBs, with the Dab-like PTB domains representing nearly 75% of proteins encoding PTB domains.	diazobenzenesulfonic acid	254-257	polypyrimidine tract binding protein 1	Homo sapiens	82-85