Proteomics

Dataset Information

0

Study of the TRAPP complexes by HDX-MS

ABSTRACT: Use of HDX-MS to study the allosteric and structural differences between the TRAPPII and TRAPPIII complex in the presence and absence of membrane and rab GTPases

INSTRUMENT(S): impact HD

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: John Burke  

LAB HEAD: Dr. John Burke

PROVIDER: PXD025928 | Pride | 2021-09-22

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
06_11_20_NHHDX5_T2_Apo_3s_1_0_01_15125.d.rar Other
06_11_20_NHHDX5_T2_Mem_3s_1_0_01_15127.d.rar Other
06_11_20_NHHDX5_T2_ND_0_01_15121.d.rar Other
06_11_20_NHHDX5_T3_Apo_3s_1_0_01_15129.d.rar Other
06_11_20_NHHDX5_T3_Mem_3s_1_0_01_15133.d.rar Other
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Publications

Biochemical Insight into Novel Rab-GEF Activity of the Mammalian TRAPPIII Complex.

Harris Noah J NJ   Jenkins Meredith L ML   Dalwadi Udit U   Fleming Kaelin D KD   Nam Sung-Eun SE   Parson Matthew A H MAH   Yip Calvin K CK   Burke John E JE  

Journal of molecular biology 20210703 18

Transport Protein Particle complexes (TRAPP) are evolutionarily conserved regulators of membrane trafficking, with this mediated by their guanine nucleotide exchange factor (GEF) activity towards Rab GTPases. In metazoans evidence suggests that two different TRAPP complexes exist, TRAPPII and TRAPPIII. These two complexes share a common core of subunits, with complex specific subunits (TRAPPC9 and TRAPPC10 in TRAPPII and TRAPPC8, TRAPPC11, TRAPPC12, TRAPPC13 in TRAPPIII). TRAPPII and TRAPPIII ha  ...[more]

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