{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,22]],"date-time":"2026-01-22T23:51:13Z","timestamp":1769125873613,"version":"3.49.0"},"reference-count":23,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2023,6,7]],"date-time":"2023-06-07T00:00:00Z","timestamp":1686096000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100001411","name":"Indian Council of Medical Research","doi-asserted-by":"publisher","award":["5\/10\/15\/CAR\u2010SMVDV\/2018\u2010RBMCH"],"award-info":[{"award-number":["5\/10\/15\/CAR\u2010SMVDV\/2018\u2010RBMCH"]}],"id":[{"id":"10.13039\/501100001411","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["analyticalsciencejournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Cell Biochemistry &amp;amp; Function"],"published-print":{"date-parts":[[2023,8]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Follicle\u2010stimulating hormone receptor (FSHR) belongs to the family of G\u2010protein coupled receptors and acts as a cognate receptor for follicle\u2010stimulating hormone (FSH). Among the various polymorphic changes reported in FSHR, rs6165 polymorphism leading to Ala307Thr variation in the extracellular domain of the FSHR (FSHR<jats:sub>ED<\/jats:sub>) is widely reported. Therefore we attempted to evaluate the functional implications of this variation by studying its effects on FSHR<jats:sub>ED<\/jats:sub> structure as well as FSH binding. Our atomic\u2010scale investigations reveal that the hinge region, a key hormone interaction site in the extracellular domain of Wt FSHR, exhibits significantly more flexibility compared with the variant structure. Moreover, the Wt receptor in complex with FSH was observed to form a pocket\u2010like structure in its hinge region whereas such a structure was not detected in the variant. The study further reveals that the key residue, sTyr335, required for FSH recognition and FSHR activation, exhibits lower binding free energy in the variant structure as compared to the Wt. In conclusion, our results point out that Ala307Thr variation leads to structural and conformational anomalies in FSHR<jats:sub>ED<\/jats:sub> which may alter its FSH binding and affect its activation.<\/jats:p>","DOI":"10.1002\/cbf.3819","type":"journal-article","created":{"date-parts":[[2023,6,8]],"date-time":"2023-06-08T01:01:35Z","timestamp":1686186095000},"page":"633-641","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Ala307Thr variation modulates FSHR structure and impairs its binding affinity for FSH: Implications in polycystic ovarian syndrome"],"prefix":"10.1002","volume":"41","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3721-0613","authenticated-orcid":false,"given":"Asif","family":"Amin","sequence":"first","affiliation":[{"name":"ICMR Centre for Advanced Research, Department of Biotechnology University of Kashmir Srinagar J&amp;K India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0292-240X","authenticated-orcid":false,"given":"Asif","family":"Lone","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Deshbandhu College University of Delhi New Delhi India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Umer Majeed","family":"Wani","sequence":"additional","affiliation":[{"name":"ICMR Centre for Advanced Research, Department of Biotechnology University of Kashmir Srinagar J&amp;K India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Faizah","family":"Farooq","sequence":"additional","affiliation":[{"name":"ICMR Centre for Advanced Research, Department of Biotechnology University of Kashmir Srinagar J&amp;K India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ruchi","family":"Shah","sequence":"additional","affiliation":[{"name":"ICMR Centre for Advanced Research, Department of Biotechnology 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