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Conformational changes in protein loops and helices induced by post-translational phosphorylation.
(2006) PLoS Comput Biol 2
PubMed: 16628247 | PubMedCentral: PMC1440919 | DOI: 10.1371/journal.pcbi.0020032
Accession Numbers The Protein Data Bank ( http://www.rcsb.org/pdb ) accession numbers for the proteins discussed in this paper are as follows: β PGM, (PDB ID: 1LVH); CDK2, phosphorylated (PDB ... D: 1JST); CDK2, unphosphorylated (PDB ID: 1FIN); CDK2/KAP complex (PDB ID: 1FQ1); cyclin A (PDB ID: 1B39); ERK2, phosphorylated (PDB ID: 2ERK); ERK2, unphosphorylated (PDB ID: 1ERK); FixJ, phosphorylated (PDB ID: 1D5W); FixJ, unphosphorylated (PDB ID: 1DCK); GLM, (PDB ID: 1MKI); Hpr, phosphorylated (PDB ID: 1FU0); Hpr, unphosphorylated (PDB ID: 1PTF); LCK, (PDB ID: 3LCK); Pim1, (PDB ID: 2BIK); PMM, (PDB ID: 1K35); Psp, phosphorylated (PDB ID: 1J97); Psp, unphosphorylated (PDB ID: 1L7O); P38 γ, (PDB ID: 1CM8); SpoIIAA, phosphorylated (PDB ID: 1H4X); and SpoIIAA, unphosphorylated (PDB ID: 1H4Z); Spo0A, (PDB ID: 1QMP).
Publication Year: 2006
The scientific impact of the Structural Genomics Consortium: a protein family and ligand-centered approach to medically-relevant human proteins.
(2007) J Struct Funct Genomics 8
PubMed: 17932789 | PubMedCentral: PMC2140095 | DOI: 10.1007/s10969-007-9027-2
Cancer e Other-NAK STK10 2J7T 2.0 SU11274 Not known STE DAPK3 2J90 2.0 Pyridone 6 Cancer, Inflammation CAMK CAMK1G 2JAM 1.7 SU11652 Not known CAMK CAMK1D 2JC6 2.5 GSK inhibitor XIII Genetic CAMK a PAK... also deposited as an apo-structure in two different spacegroups: 2BVA, 2J01 b Structures with different inhibitors and substrate: PIM1: 2BIK, 2BZH,2BZI, 2BZJ, 2BZK, 2C3I, 2BIL, 2J2I; SLK: 2JA0 c CLK3 also deposited as phosphorylated protein: pdb-code: 2EXE.
Publication Year: 2007
Binding of protein kinase inhibitors to synapsin I inferred from pair-wise binding site similarity measurements.
(2010) PLoS One 5
PubMed: 20808948 | PubMedCentral: PMC2922380 | DOI: 10.1371/journal.pone.0012214
PDB a d2 b Name HET c 2oxd 0.1008 Casein kinase II subunit alpha K32 2oxx 0.1038 Casein kinase II subunit alpha K22 1yi3 0.1056 Proto-oncogene serine/threonine-protein kinase Pim-1 LY2 1tqm 0.1083 RIO... type serine/threonine-protein kinase Rio2 ANP 3cy3 0.1176 Proto-oncogene serine/threonine-protein kinase Pim-1 JN5 3bgz 0.1199 Proto-oncogene serine/threonine-protein kinase Pim-1 VX3 3cy2 0.1233 Proto-oncogene serine/threonine-protein kinase Pim-1 MB9 2bik 0.1327 Proto-oncogene serine/threonine-protein kinase Pim-1 BI1 2c1a 0.1339 Protein kinase A I5S 1xr1 0.1350 Proto-oncogene serine/threonine-protein kinase Pim-1 ANP 1bl6 0.1368 Mitogen-activated protein kinase 14 SB6 1q8u 0.1385 cAMP-dependent protein kinase catalytic subunit alpha H52 3bi6 0.1388 Wee1-like protein kinase 396 3biz 0.1395 Wee1-like protein kinase 61E 2i0e 0.1400 Protein kinase C beta type PDS 1cm8 0.1405 Mitogen-activated protein kinase 12 ANP 2uzv 0.1423 cAMP-dependent protein kinase catalytic subunit alpha SS5 1yi4 0.1456 Proto-oncogene serine/threonine-protein kinase Pim-1 ADN 2hen 0.1467 Ephrin type-B receptor 2 ADP 2rkp 0.1474 Casein kinase II subunit alpha RFZ 2ojg 0.1481 Mitogen-activated protein kinase 1 19A 2z7s 0.1481 Ribosomal protein S6 kinase alpha-1 P01 2csn 0.1482 Casein kinase I homolog 1 CKI 1yhs 0.1483 Proto-oncogene serine/threonine-protein kinase Pim-1 STU 1mu 0.1508 Serine/threonine-protein kinase 6 ADN a PDB entry  .
Publication Year: 2010
OGlcNAcylation and phosphorylation have similar structural effects in ?-helices: post-translational modifications as inducible start and stop signals in ?-helices, with greater structural effects on threonine modification.
(2014) Biochemistry 53
PubMed: 24641765 | PubMedCentral: PMC4004263 | DOI: 10.1021/bi500117c
Analysis of phosphoserine and phosphothreonine residues in α-helices in high-resolution structures in the PDB (structures at ≤2.4 Å, 90% sequence identity cutoff) indicated a s... rong preference for phosphoserine and phosphothreonine to be at or near the helical N-terminus when they were present in α-helices (pSer: 1h4x, 2fwn, 3mk1, 3ql6, 2w5w, 2bik, 3f3z, 1mki, and 3qic; pThr: 3ot9, 4iza, 2ga3, 2jfl, 2w8d, 2wtv, and 3u02; PDB entry 1r0z was the only example among these structures in which an α-helical phosphorylated residue was outside the first turn of the α-helix).
Publication Year: 2014
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