1MQ8: AlphaL I domain

Crystal structure of alphaL I domain in complex with ICAM-1. Determined by X-ray diffraction at 3.3 Å resolution. Released 14 Jan 2003.

Method: X-ray diffraction
Resolution: 3.3 Å
Organism: Homo sapiens
Chains: 4
Atoms: 5,854
Mol. weight: 106.26 kDa
Ligands: MG, NAG
Released: 14 Jan 2003

Explore 1MQ8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1MQ8 contains 18 α-helices and 65 β-strands across 4 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: 2 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	2-5	4	1
β-strand	8-11	4	2
β-strand	16-23	8	1
β-strand	30-34	5	3
α-helix	38-39	2
β-strand	49-55	7	1
β-strand	64-68	5	3
β-strand	73-77	5	3
β-strand	79-82	4	2
β-strand	84	1	4
β-strand	91	1	5
β-strand	97	1	6
β-strand	105-110	6	5
β-strand	114	1	4
β-strand	119-124	6	7
β-strand	129-134	6	7
β-strand	137	1	5
β-strand	140-145	6	5
β-strand	156-157	2	8
β-strand	158-164	7	7
α-helix	166-168	3
β-strand	172-175	4	7
β-strand	180-181	2	8
β-strand	183	1	6

Chain B: 7 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	131-136	6	9
β-strand	137	1	10
β-strand	139	1	11
α-helix	146-157	12
α-helix	159-161	3
β-strand	167	1	9
β-strand	170-171	2	9
β-strand	173	1	10
β-strand	179-181	3	9
α-helix	183-186	4
β-strand	204	1	11
α-helix	209-217	9
α-helix	222-225	4
β-strand	232-237	6	9
α-helix	249-251	3
β-strand	255	1	9
β-strand	259	1	9
α-helix	299-302	4

Chain C: 2 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	2-5	4	12
β-strand	8-11	4	13
β-strand	16-23	8	12
β-strand	30-34	5	14
α-helix	38-39	2
β-strand	41	1	12
β-strand	49-55	7	12
β-strand	64-68	5	14
β-strand	73-77	5	14
β-strand	79-82	4	13
β-strand	84	1	15
β-strand	91	1	16
β-strand	97	1	17
β-strand	105-110	6	16
β-strand	114	1	15
β-strand	119-124	6	18
β-strand	129-134	6	18
β-strand	137	1	16
β-strand	140-145	6	16
β-strand	156-157	2	19
β-strand	158-164	7	18
α-helix	166-168	3
β-strand	172-175	4	18
β-strand	180-181	2	19
β-strand	183	1	17

Chain D: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	131-137	7	20
β-strand	139	1	21
α-helix	146-157	12
α-helix	159-161	3
β-strand	167	1	20
β-strand	170-173	4	20
β-strand	177-181	5	20
α-helix	183-186	4
β-strand	204	1	21
α-helix	209-217	9
α-helix	222-225	4
β-strand	232-237	6	20
α-helix	249-251	3
β-strand	255	1	20
β-strand	259	1	20
α-helix	299-302	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
intercellular adhesion molecule-1	A, C	protein	291	Homo sapiens	P05362 (AlphaFold model)
Integrin alpha-L	B, D	protein	177	Homo sapiens	P20701 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1MQ8_1 intercellular adhesion molecule-1 (chains A, C)
QTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQED
SQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKNLTLRCQVEGGAPRANLT
VVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGANFSCRTELDLRPQGLELFENTSAPY
QLQTFVLPATPPQLVSPRVLEVDTQGTVVCSLDGLFPVSEAQVHLALGDQRLNPTVTYGN
DSFSAKASVSVTAEDEGTQRLTCAVILGNQSQETLQTVTIYSFPAPNVILT

Sequence of entity 2 (B, D), FASTA

>1MQ8_2 Integrin alpha-L (chains B, D)
VDLVFLFDGSMSLQPDEFQKILDFMKDVMKKCSNTSYQFAAVQFSTSYKTEFDFSDYVKR
KDPDALLKHVKHMLLLTNTFGAINYVATEVFREELGARPDATKVLIIITDGEATDSGNID
AAKDIIRYIIGIGKHFQTKESQETLHKFASKPASEFVKILDTFEKLKDLCTELQKKI

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	4

Primary citation

Structures of the aL I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation. Shimaoka, M., Xiao, T., Liu, J.-H. et al. Cell (2003) 112:99-111. DOI 10.1016/S0092-8674(02)01257-6 · PubMed

Other PDB entries of the same protein (UniProt P05362 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1IAM 2.1 Å, Structure of the two amino-terminal domains of human intercellular adhesion molecule-1,…
7BG7 2.4 Å, HRV14 in complex with its receptor ICAM-1
2OZ4 2.7 Å, Structural Plasticity in IgSF Domain 4 of ICAM-1 Mediates Cell Surface Dimerization
5MZA 2.78 Å, The DBLb domain of PF11_0521 PfEMP1 bound to human ICAM-1
1IC1 3.0 Å, The crystal structure for the N-terminal two domains of icam-1
1P53 3.06 Å, The Crystal Structure of ICAM-1 D3-D5 fragment
1D3L 3.25 Å, D1D2-icam-1 fully glycosylated, variation of D1-D2 interdomain angle in different…
3TCX 3.6 Å, Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain…
6S8U 3.67 Å, Structure of the PfEMP1 IT4var13 DBLbeta domain bound to ICAM-1
6EIT 3.9 Å, Coxsackievirus A24v in complex with the D1-D2 fragment of ICAM-1
1Z7Z 8.0 Å, Cryo-em structure of human coxsackievirus A21 complexed with five domain icam-1kilifi
1D3I 26.0 Å, cryo-EM structure of human rhinovirus 14 (HRV14) complexed with a two-domain fragment of…

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