8WHH: Se-Met derivative CLASP2

Crystal structure of Se-Met derivative CLASP2 in complex with CLIP170. Determined by X-ray diffraction at 3.8 Å resolution. Released 28 Aug 2024.

Method: X-ray diffraction
Resolution: 3.8 Å
Organism: Homo sapiens
Chains: 8
Atoms: 10,075
Mol. weight: 157.47 kDa
Released: 28 Aug 2024

Explore 8WHH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8WHH contains 60 α-helices and 0 β-strands across 8 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	1257-1265	9
α-helix	1272-1287	16
α-helix	1294-1308	15
α-helix	1314-1330	17
α-helix	1332-1335	4
α-helix	1339-1349	11
α-helix	1355-1371	17
α-helix	1374-1387	14
α-helix	1388-1389	2
α-helix	1392-1404	13
α-helix	1409-1427	19
α-helix	1432-1449	18
α-helix	1450-1457	8
α-helix	1462-1476	15

Chain B: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	1258-1265	8
α-helix	1272-1287	16
α-helix	1294-1308	15
α-helix	1314-1330	17
α-helix	1332-1335	4
α-helix	1339-1349	11
α-helix	1355-1369	15
α-helix	1374-1387	14
α-helix	1388-1389	2
α-helix	1392-1404	13
α-helix	1409-1427	19
α-helix	1432-1449	18
α-helix	1450-1457	8
α-helix	1462-1476	15

Chain C: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	1258-1265	8
α-helix	1272-1287	16
α-helix	1294-1308	15
α-helix	1314-1330	17
α-helix	1332-1335	4
α-helix	1339-1349	11
α-helix	1355-1371	17
α-helix	1374-1387	14
α-helix	1388-1389	2
α-helix	1392-1404	13
α-helix	1409-1427	19
α-helix	1432-1449	18
α-helix	1450-1457	8
α-helix	1462-1476	15

Chain D: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	1257-1265	9
α-helix	1272-1287	16
α-helix	1294-1308	15
α-helix	1314-1330	17
α-helix	1332-1338	7
α-helix	1339-1349	11
α-helix	1355-1369	15
α-helix	1374-1387	14
α-helix	1388-1389	2
α-helix	1392-1404	13
α-helix	1409-1427	19
α-helix	1432-1449	18
α-helix	1450-1457	8
α-helix	1462-1476	15

Chain E: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	350-450	101

Chains F and H: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	350-449	100

Chain G: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	350-452	103

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
CLIP-associating protein 2	A, B, C, D	protein	235	Homo sapiens	O75122 (AlphaFold model)
CLIP1 protein	E, F, G, H	protein	111	Homo sapiens	P30622 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>8WHH_1 CLIP-associating protein 2 (chains A, B, C, D)
GPGSEFSLDHSDLVAELLKELSNHNERVEERKIALYELMKLTQEESFSVWDEHFKTILLL
LLETLGDKEPTIRALALKVLREILRHQPARFKNYAELTVMKTLEAHKDPHKEVVRSAEEA
ASVLATSISPEQCIKVLCPIIQTADYPINLAAIKMQTKVIERVSKETLNLLLPEIMPGLI
QGYDNSESSVRKACVFCLVAVHAVIGDELKPHLSQLTGSKMKLLNLYIKRAQTGS

Sequence of entity 2 (E, F, G, H), FASTA

>8WHH_2 CLIP1 protein (chains E, F, G, H)
GPGSTTALQEALKEKQQHIEQLLAERDLERAEVAKATSHVGEIEQELALARDGHDQHVLE
LEAKMDQLRTMVEAADREKVELLNQLEEEKRKVEDLQFRVEEESITKGDLE

Primary citation

CLASP-mediated competitive binding in protein condensates directs microtubule growth. Jia, X., Lin, L., Guo, S. et al. Nat Commun (2024) 15:6509-6509. DOI 10.1038/s41467-024-50863-3 · PubMed

Other PDB entries of the same protein (UniProt O75122 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5NR4 1.2 Å, Crystal structure of Clasp2 TOG1 domain
8WHJ 1.4 Å, Crystal structure of CLASP2 TOG4 fused with LL5beta
8WHI 1.85 Å, Crystal structure of native CLASP2 in complex with CLIP170
3WOY 2.1 Å, Crystal structure of CLASP2 TOG domain (TOG2)
8WHK 2.4 Å, Crystal structure of CLASP2 in complex with LL5beta
8WHL 3.2 Å, Crystal structure of CLASP2 in complex with CENP-E

Browse structure collections

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