4B3Z

Structure of the human collapsin response mediator protein-1, a lung cancer suppressor

Summary for 4B3Z

• Entry DOI: 10.2210/pdb4b3z/pdb
• Descriptor: DIHYDROPYRIMIDINASE-RELATED PROTEIN 1 (1 entity in total)
• Functional Keywords: hydrolase, semaphorin 3a, tim barrel, non-small-cell lung cancer, lung cancer suppressor
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm : Q14194
• Total number of polymer chains: 4
• Total formula weight: 249026.41

Authors

Liu, S.H.,Lin, Y.H.,Huang, S.F.,Niou, Y.K.,Huang, L.L.,Chen, Y.J. (deposition date: 2012-07-27, release date: 2013-08-07, Last modification date: 2023-12-20)

Primary citation

Liu, S.H.,Huang, S.F.,Hsu, Y.L.,Pan, S.H.,Chen, Y.J.,Lin, Y.H.
Structure of Human Collapsin Response Mediator Protein 1: A Possible Role of its C-Terminal Tail.
Acta Crystallogr.,Sect.F, 71:938-, 2015

PubMed Abstract: Collapsin response mediator protein 1 (CRMP-1) is the first identified member of the CRMP family and is crucial for both the mediation of neuronal differentiation and in suppressing the invasion of lung cancer. The crystal structure of full-length human CRMP-1 was determined at a resolution of 3 Å. Human CRMP-1 comprises a tetrameric assembly; its overall structure is similar to that of mouse CRMP-1, but the measured electron density of the C-terminal residues 488-496 show a randomly coiled link that connects the protomers to each other, within which residues 497-572 are proteolytically susceptible in vivo. Deletion of residues 472-572 by thrombin in vitro not only releases a randomly coiled tail but also transduces observable structural changes of CRMP-1, as revealed by analytical size-exclusive chromatography and circular dichroism spectra. These results indicate a possible alternative role in CRMP dynamics and function.

PubMed: 26249678
DOI: 10.1107/S2053230X15009243

Experimental method

X-RAY DIFFRACTION (3.05 Å)