Dataset Information

Assembly of a nuclear lamin coil 2 fragment

ABSTRACT: Nuclear structure and function are governed by lamins, which are intermediate filaments mostly consisting of α-helices. Different lamin assembly models have been proposed based on low resolution or fragmented structures. However, their assembly mechanisms at the molecular level are poorly understood. The structure shows the anti-parallel arrangement of two coiled-coil dimers, which is important for the assembly process. We further discovered a new interaction of a coil 2 by using chemical cross-linking and mass analysis, of which the results were deposited in the PRIDE identifier PXD013144. Here we showed that a cysteine-substituted coil 2 R388C segment (286-400 amino acid residues of lamin) was dimerized by the chemical crosslinking. Our findings also provide a molecular basis for the assembly mechanisms of other intermediate filaments.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Fibroblast

DISEASE(S): Progeria

SUBMITTER: Yong-Hak Kim

LAB HEAD: Yong-Hak Kim

PROVIDER: PXD014029 | Pride | 2025-12-15

REPOSITORIES: Pride

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Publications

Structural basis for lamin assembly at the molecular level.

Ahn Jinsook J Jo Inseong I Kang So-Mi SM Hong Seokho S Kim Suhyeon S Jeong Soyeon S Kim Yong-Hak YH Park Bum-Joon BJ Ha Nam-Chul NC

Nature communications 20190821 1

Nuclear structure and function are governed by lamins, which are intermediate filaments that mostly consist of α-helices. Different lamin assembly models have been proposed based on low resolution and fragmented structures. However, their assembly mechanisms are still poorly understood at the molecular level. Here, we present the crystal structure of a long human lamin fragment at 3.2 Å resolution that allows the visualization of the features of the full-length protein. The structure shows an an ...[more]

PMID: 31434876

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			Action	DRS
	coil2-dimer_merge.pep.xml	Pepxml
	coil2dimer-1.raw	Raw
	coil2dimer-2.raw	Raw
	coil2dimer_merge.msf	Msf