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spinqualitylabelsall models Human lamini integrin binding domain. Subunit α-5 (grey, yellow), subunit β-1 (green, light pink), subunit γ-1 (yellow, cyan) and Ca+2 (green)(PDB code 5xau) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Disease 3 Relevance 4 Structural highlights Function Laminins (LAM) are a family of glycoproteins that provide the integral part of the structural scaffolding of basement membranes in almost every animal tissue. Laminins are heterotrimers containing α-, β- and γ-subunits[1]. Laminins are essential for early embryonic development and organogenesis and have crucial functions in tissues like muscles, lung, skin, kidney and nerve[2]. Several members of the integrin family serve as laminin receptors on a variety of cell types[3]. - Disease Relevance Serum concentration of laminin is increased in patients with inflammatory bowel disease hence can be used as a marker for sustained inflammation[4]. Laminin was found to have an anti-amyloidogenic effect and γmay be of therapeutic value in Alzheimer Disease[5]. Laminin-111 was found to be a highly therapeutic agent in mice with Duchenne muscular dystrophy[6]. Structural highlights

3D structures of laminin

Updated on 16-April-2020

4yeq, 4yep - hLAM subunit α-2 L4b domain 1177-1379 - human
5xau - hLAM integrin-binding domain subunit α-5 6559-3327 + hLAM subunit β-1 1714-1786 + hLAM subunit γ-1 1528-6097 (mutant)
5lf2 - rLAM subunit β-2 LE5-LF-LE6 domain 523-833 - rat
2jd4 - mLAM subunit α-1 LG4-5 domain 2706-3084 (mutant) - mouse
2wj8 - mLAM subunit α-2 LG1-3 domain 2136-2746
5ik7, 5ik4, 5ik8, 5ik5 - mLAM subunit α-2 LG4-5 domain 2729-3118
1dyk, 1okq - mLAM subunit α-2 LG4-5 domain 2729-3118 (mutant)
1qu0 - mLAM subunit α-2 LG5 domain 2932-3106 (mutant)
2y38 - mLAM subunit α-5 LN-LEA1-2 domain 44-433
1tle - mLAM subunit γ-1 LE domain 824-881 - NMR
4aqt - mLAM subunit γ-1 LN-LE2 domain 53-395
4aqs - mLAM subunit γ-1 LN-LE4 domain 22-542
1klo - mLAM subunit γ-1 module III 3-5 771-932
1npe - mLAM subunit γ-1 module III 3-5 + nidogen G3 YWTD domain
5mc9 - mLAM integrin-binding domain subunit α-1 2079-2707 + mLAM subunit β-1 1735-1786 + mLAM subunit γ-1 1548-1507

References

1. ↑ Colognato H, Yurchenco PD. Form and function: the laminin family of heterotrimers. Dev Dyn. 2000 Jun;218(2):213-34. doi:, 10.1002/(SICI)1097-0177(200006)218:2<213::AID-DVDY1>3.0.CO;2-R. PMID:10842354 doi:<213::AID-DVDY1>3.0.CO;2-R http://dx.doi.org/10.1002/(SICI)1097-0177(200006)218:2<213::AID-DVDY1>3.0.CO;2-R
2. ↑ Durbeej M. Laminins. Cell Tissue Res. 2010 Jan;339(1):259-68. doi: 10.1007/s00441-009-0838-2. Epub, 2009 Aug 20. PMID:19693542 doi:http://dx.doi.org/10.1007/s00441-009-0838-2
3. ↑ Belkin AM, Stepp MA. Integrins as receptors for laminins. Microsc Res Tech. 2000 Nov 1;51(3):280-301. doi:, 10.1002/1097-0029(20001101)51:3<280::AID-JEMT7>3.0.CO;2-O. PMID:11054877 doi:<280::AID-JEMT7>3.0.CO;2-O http://dx.doi.org/10.1002/1097-0029(20001101)51:3<280::AID-JEMT7>3.0.CO;2-O
4. ↑ Koutroubakis IE, Petinaki E, Dimoulios P, Vardas E, Roussomoustakaki M, Maniatis AN, Kouroumalis EA. Serum laminin and collagen IV in inflammatory bowel disease. J Clin Pathol. 2003 Nov;56(11):817-20. doi: 10.1136/jcp.56.11.817. PMID:14600124 doi:http://dx.doi.org/10.1136/jcp.56.11.817
5. ↑ Morgan C, Inestrosa NC. Interactions of laminin with the amyloid beta peptide. Implications for Alzheimer's disease. Braz J Med Biol Res. 2001 May;34(5):597-601. doi:, 10.1590/s0100-879x2001000500006. PMID:11323745 doi:http://dx.doi.org/10.1590/s0100-879x2001000500006
6. ↑ Rooney JE, Gurpur PB, Burkin DJ. Laminin-111 protein therapy prevents muscle disease in the mdx mouse model for Duchenne muscular dystrophy. Proc Natl Acad Sci U S A. 2009 May 12;106(19):7991-6. doi:, 10.1073/pnas.0811599106. Epub 2009 Apr 28. PMID:19416897 doi:http://dx.doi.org/10.1073/pnas.0811599106