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"metadata": {
"accession": "PS52047",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "profile",
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"name": {
"name": "Integrins beta chain EGF (I-EGF) domain profile",
"short": "I_EGF_2"
},
"description": [
{
"text": "<p>Integrins [[cite:PUB00000811]][[cite:PUB00001505]] are a large family of cell surface receptors that mediate cell\nto cell as well as cell to matrix adhesion. Some integrins recognize the R-G-D\nsequence in their extracellular matrix protein ligand.\nStructurally, integrins consist of a dimer of an alpha and a beta chain. Each\nsubunit has a large N-terminal extracellular domain followed by a\ntransmembrane domain and a short C-terminal cytoplasmic region. Some receptors\nshare a common beta chain while having different alpha chains. The sequence of\na number of different beta chains has been determined and are listed below:\n\n - Integrin beta-1, which associates with alpha-1 to form a laminin receptor,\n with alpha-2 to form a collagen receptor, with alpha-4 to interact with\n VCAM-1, with alpha-5 to form a fibronectin receptor, and with alpha-8.\n - Integrin beta-2, which associates with alpha-L (LFA-1) to interact with\n ICAM-1, and with alpha-M (MAC-1) or alpha-X (p150,95) to form the receptor\n for the iC3b fragment of the third complement component.\n - Integrin beta-3, which associates with alpha-IIB to form a receptor for\n fibrinogen, fibronectin, vitronectin and VWF, and with alpha-V to form a\n vitronectin receptor.\n - Integrin beta-4, which associates with alpha-6.\n - Integrin beta-5, which associates with alpha-V.\n - Integrin beta-6 [[cite:PUB00002561]].\n - Integrin beta-7 [[cite:PUB00002637]].\n - Integrin beta-8, which associates with alpha-V [[cite:PUB00002660]].\n - The Drosophila myospheroid protein, a probable integrin beta chain.\n\nThe C-terminus of the extracellular region of all the integrin beta chains has\nfour cysteine-rich tandem repeats of forty amino acids, which are variants of\nthe EGF-like domain, termed integrin- or I-EGF domains. The\nI-EGF domain is a small globular domain mainly composed by loops with a small\nanti-parallel beta-sheet constituted of two beta-strands (see {PDB:1L3Y}. The\nstructure is stabilized by four disulfide bonds between the first and fifth,\nsecond and fourth, third and sixth, and seventh and eighth Cys residues. Three\ndisulfide bonds are shared with classical EGF-like domains. The disulfide\nunique to I-EGF domains links the N-terminus to the turn between the two beta-\nstrands. Compared to classical EGF-like modules with three disulfide bonds,\nthe I-EGF module is less elongated, with a nosecone-like shape. The anti-\nparallel sheet between the two beta-strands is shortened because four highly\nconserved residues among classical EGF-like modules are deleted in I-EGF\nmodules. I-EGF repeats in the integrin beta subunit stalk region relay\nactivation signals to the ligand-binding headpiece [[cite:PUB00002660]][[cite:PUB00026914]].\n\nWe have developed a pattern from a section of the I-EGF domain that includes\nfive of the conserved cysteines. We also developed a profile which covers the\nentire I-EGF domain.</p>",
"llm": false,
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}
],
"wikipedia": null,
"literature": {
"PUB00002561": {
"PMID": 2365683,
"ISBN": null,
"volume": "265",
"issue": "20",
"year": 1990,
"title": "Complete amino acid sequence of a novel integrin beta subunit (beta 6) identified in epithelial cells using the polymerase chain reaction.",
"URL": null,
"raw_pages": "11502-7",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Sheppard D",
"Rozzo C",
"Starr L",
"Quaranta V",
"Erle DJ",
"Pytela R."
],
"DOI_URL": "http://intl.jbc.org/cgi/content/abstract/265/20/11502"
},
"PUB00002660": {
"PMID": 1918072,
"ISBN": null,
"volume": "266",
"issue": "29",
"year": 1991,
"title": "Cloning and expression of a divergent integrin subunit beta 8.",
"URL": null,
"raw_pages": "19650-8",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Moyle M",
"Napier MA",
"McLean JW."
],
"DOI_URL": "http://intl.jbc.org/cgi/reprint/266/29/19650.pdf"
},
"PUB00026914": {
"PMID": 11896403,
"ISBN": null,
"volume": "9",
"issue": "4",
"year": 2002,
"title": "Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation.",
"URL": null,
"raw_pages": "282-7",
"medline_journal": "Nat Struct Biol",
"ISO_journal": "Nat. Struct. Biol.",
"authors": [
"Beglova N",
"Blacklow SC",
"Takagi J",
"Springer TA."
],
"DOI_URL": "http://dx.doi.org/10.1038/nsb779"
},
"PUB00000811": {
"PMID": 3028640,
"ISBN": null,
"volume": "48",
"issue": "4",
"year": 1987,
"title": "Integrins: a family of cell surface receptors.",
"URL": null,
"raw_pages": "549-54",
"medline_journal": "Cell",
"ISO_journal": "Cell",
"authors": [
"Hynes RO."
],
"DOI_URL": "http://dx.doi.org/10.1016/0092-8674(87)90233-9"
},
"PUB00002637": {
"PMID": 2040616,
"ISBN": null,
"volume": "266",
"issue": "17",
"year": 1991,
"title": "Complete amino acid sequence of an integrin beta subunit (beta 7) identified in leukocytes.",
"URL": null,
"raw_pages": "11009-16",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Erle DJ",
"Ruegg C",
"Sheppard D",
"Pytela R."
],
"DOI_URL": "http://intl.jbc.org/cgi/reprint/266/17/11009.pdf"
},
"PUB00001505": {
"PMID": 2199285,
"ISBN": null,
"volume": "4",
"issue": "11",
"year": 1990,
"title": "Integrins and other cell adhesion molecules.",
"URL": null,
"raw_pages": "2868-80",
"medline_journal": "FASEB J",
"ISO_journal": "FASEB J.",
"authors": [
"Albelda SM",
"Buck CA."
],
"DOI_URL": "http://www.fasebj.org/cgi/content/abstract/4/11/2868"
}
},
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"interactions": 0,
"matches": 36929,
"pathways": 0,
"proteins": 13478,
"proteomes": 1215,
"sets": 0,
"structural_models": {
"alphafold": 11372,
"bfvd": 0
},
"structures": 135,
"taxa": 4211
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
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"representative_structure": null
}
}
